M00136
type: Enzyme
rlcp: p358
cath: 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A
cath: Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
cath: Immunoglobulin-like
cath: Phosphorylase Kinase; domain 1
cath: Transferase(Phosphotransferase); domain 1
ec: https://purl.uniprot.org/enzyme/2.7.10.1
uniprot: P08069
kegg enzyme: receptor protein-tyrosine kinase
kegg enzyme: AATK
kegg enzyme: AATYK
kegg enzyme: AATYK2
kegg enzyme: AATYK3
kegg enzyme: ACH
kegg enzyme: ALK
kegg enzyme: anaplastic lymphoma kinase
kegg enzyme: ARK
kegg enzyme: ATP:protein-tyrosine O-phosphotransferase (ambiguous)
kegg enzyme: AXL
kegg enzyme: Bek
kegg enzyme: Bfgfr
kegg enzyme: BRT
kegg enzyme: Bsk
kegg enzyme: C-FMS
kegg enzyme: CAK
kegg enzyme: CCK4
kegg enzyme: CD115
kegg enzyme: CD135
kegg enzyme: CDw135
kegg enzyme: Cek1
kegg enzyme: Cek10
kegg enzyme: Cek11
kegg enzyme: Cek2
kegg cofactor: Magnesium
kegg substrate: ATP
kegg substrate: [Protein]-L-tyrosine
kegg product: ADP
kegg product: [Protein]-L-tyrosine phosphate
pdb: 1igrA01
pdb: 1igrA02
pdb: 1igrA03
pdb: 1jqhA01
pdb: 1jqhB01
pdb: 1jqhC01
pdb: 1k3aA01
pdb: 1m7nA01
pdb: 1m7nB01
pdb: 1p4oA01
pdb: 1p4oB01
pdb: 1jqhA02
pdb: 1jqhB02
pdb: 1jqhC02
pdb: 1k3aA02
pdb: 1m7nA02
pdb: 1m7nB02
pdb: 1p4oA02
pdb: 1p4oB02
references: Analysis of the interaction of IGF-I analogs with the IGF-I receptor and IGF binding proteins.
references: The insulin-like growth factor-I receptor. Structure, ligand-binding mechanism and signal transduction.
references: Tyrosine residues in the C-terminal domain of the insulin-like growth factor-I receptor mediate mitogenic and tumorigenic signals.
references: Crystallization of the first three domains of the human insulin-like growth factor-1 receptor.
references: Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor.
references: C-terminal Src kinase associates with ligand-stimulated insulin-like growth factor-I receptor.
references: Autophosphorylation of the insulin-like growth factor I receptor cytoplasmic domain.
references: Regulation of survival signals from the insulin-like growth factor-I receptor.
references: Cys 786 and Cys 776 in the posttranslational processing of the insulin and IGF-I receptors.
references: Specificity in ligand binding and intracellular signalling by insulin and insulin-like growth factor receptors.
references: Dimerization-induced activation of soluble insulin/IGF-1 receptor kinases: an alternative mechanism of activation.
references: Surfing the insulin signaling web.
references: A PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptor.
references: Cooperative regulation of the invasive and metastatic phenotypes by different domains of the type I insulin-like growth factor receptor beta subunit.
references: Alanine scanning mutagenesis of a type 1 insulin-like growth factor receptor ligand binding site.
references: The three dimensional structure of the type I insulin-like growth factor receptor.
references: Structure and autoregulation of the insulin-like growth factor 1 receptor kinase.
references: Structure-function studies of an IGF-I analogue that can be chemically cleaved to a two-chain mini-IGF-I.
references: Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activation.
references: Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity.
comment: The E.C. was transferred from 2.7.1.112 to 2.7.10.1. This protein is a receptor enzyme, insulin-like growth factor I receptor, composed of two chains, alpha and beta. PDB structure, 1igr, corresponds to the N-terminal domains of the alpha chain. The beta chain is composed of an extracellular reagion, transmembrane region, and a cytoplasmic region. The extracellular region contains a fibronectin type-III domain, whilst the cytoplasmic region has got a kinase domain. PDB structures, 1jqh, 1k3a, 1m7n & 1p4o, correspond to the kinase domain. According to the literature [17] & [19], Asp1105 (of PDB entry 1k3a) seemes to be a general base, which can activate the acceptor group, the hydroxyl group of substrate tyrosine, which in turn would make a nucleophilic attack on the transferred group, gamma-phosphate group of ATP. Arg1109 also seems to interact with both the general base and the acceptor hydroxyl group. Although two magnesium ions are coordinated to the beta- and gamma-phosphates of ATP analogue in a homologous receptor enzyme, Insulin receptor kinase (see M00129), only one magnesium ion is coordinated by the alpha- and gamma-phosphates and two water molecules (see [19]).

24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.80.20.20

Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.10.220.10

Immunoglobulin-like
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.40.30

Phosphorylase Kinase; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.200.20

Transferase(Phosphotransferase); domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.510.10
catalytic domain: index.html

Magnesium
type: KeggCofactor
references: KEGG:C00305
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggSubstrate
references: KEGG:C00002
compound type: amine group
compound type: nucleotide
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

[Protein]-L-tyrosine
type: KeggSubstrate
references: KEGG:C00585
compound type: aromatic ring (only carbon atom)
compound type: peptide/protein

ADP
type: KeggProduct
references: KEGG:C00008
compound type: amine group
compound type: nucleotide
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

[Protein]-L-tyrosine phosphate
type: KeggProduct
references: KEGG:C01167
compound type: aromatic ring (only carbon atom)
compound type: peptide/protein
compound type: phosphate group/phosphate ion

1jqhA02
type: Pdb
references: 1jqh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jqh
catalytic residue: ASP 1135;ARG 1139
modified residue: ;TYR 1165;TYR 1166(auto-phosphorylation)

1jqhB02
type: Pdb
references: 1jqh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jqh
catalytic residue: ASP 1135;ARG 1139
modified residue: ;TYR 1165;TYR 1166(auto-phosphorylation)

1jqhC02
type: Pdb
references: 1jqh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jqh
catalytic residue: ASP 1135;ARG 1139
modified residue: ;TYR 1165;TYR 1166(auto-phosphorylation)

1k3aA02
type: Pdb
references: 1k3a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k3a
catalytic residue: ASP 1105;ARG 1109
modified residue: PTR 1131;PTR 1135;PTR 1136(auto-phosphorylation)

1m7nA02
type: Pdb
references: 1m7n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m7n
catalytic residue: ASP 1132;ARG 1136
modified residue: TYR 1158;TYR 1162;TYR 1163(auto-phosphorylation)

1m7nB02
type: Pdb
references: 1m7n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m7n
catalytic residue: ASP 1132;ARG 1136
modified residue: TYR 1158;TYR 1162;TYR 1163(auto-phosphorylation)

1p4oA02
type: Pdb
references: 1p4o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p4o
catalytic residue: ASP 1105;ARG 1109
modified residue: TYR 1131;TYR 1135;TYR 1136(auto-phosphorylation)

1p4oB02
type: Pdb
references: 1p4o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p4o
catalytic residue: ASP 1105;ARG 1109
modified residue: TYR 1131;TYR 1135;TYR 1136(auto-phosphorylation)

Analysis of the interaction of IGF-I analogs with the IGF-I receptor and IGF binding proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7514345
journal: Adv Exp Med Biol
volume: 343
pages: 33-40
published year: 1993
authors:
  item: Cascieri MA
  item: Bayne ML

The insulin-like growth factor-I receptor. Structure, ligand-binding mechanism and signal transduction.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7868068
journal: Horm Res
volume: 42
pages: 152-69
published year: 1994
authors:
  item: De Meyts P
  item: Wallach B
  item: Christoffersen CT
  item: Urso B
  item: Gronskov K
  item: Latus LJ
  item: Yakushiji F
  item: Ilondo MM
  item: Shymko RM

Tyrosine residues in the C-terminal domain of the insulin-like growth factor-I receptor mediate mitogenic and tumorigenic signals.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9202243
journal: Endocrinology
volume: 138
pages: 2979-88
published year: 1997
authors:
  item: Esposito DL
  item: Blakesley VA
  item: Koval AP
  item: Scrimgeour AG
  item: LeRoith D

Crystallization of the first three domains of the human insulin-like growth factor-1 receptor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9416620
journal: Protein Sci
volume: 6
pages: 2663-6
published year: 1997
authors:
  item: McKern NM
  item: Lou M
  item: Frenkel MJ
  item: Verkuylen A
  item: Bentley JD
  item: Lovrecz GO
  item: Ivancic N
  item: Elleman TC
  item: Garrett TP
  item: Cosgrove LJ
  item: Ward CW

Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9690478
journal: Nature
volume: 394
pages: 395-9
published year: 1998
authors:
  item: Garrett TP
  item: McKern NM
  item: Lou M
  item: Frenkel MJ
  item: Bentley JD
  item: Lovrecz GO
  item: Elleman TC
  item: Cosgrove LJ
  item: Ward CW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

C-terminal Src kinase associates with ligand-stimulated insulin-like growth factor-I receptor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10026153
journal: J Biol Chem
volume: 274
pages: 5422-8
published year: 1999
authors:
  item: Arbet-Engels C
  item: Tartare-Deckert S
  item: Eckhart W

Autophosphorylation of the insulin-like growth factor I receptor cytoplasmic domain.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11162456
journal: Biochem Biophys Res Commun
volume: 279
pages: 955-60
published year: 2000
authors:
  item: Lopaczynski W
  item: Terry C
  item: Nissley P

Regulation of survival signals from the insulin-like growth factor-I receptor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10816097
journal: Biochem Soc Trans
volume: 28
pages: 47-51
published year: 2000
authors:
  item: O'Connor R
  item: Fennelly C
  item: Krause D

Cys 786 and Cys 776 in the posttranslational processing of the insulin and IGF-I receptors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11162597
journal: Biochem Biophys Res Commun
volume: 280
pages: 836-41
published year: 2001
authors:
  item: Maggi D
  item: Cordera R

Specificity in ligand binding and intracellular signalling by insulin and insulin-like growth factor receptors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11498020
journal: Biochem Soc Trans
volume: 29
pages: 513-25
published year: 2001
authors:
  item: Siddle K
  item: Urso B
  item: Niesler CA
  item: Cope DL
  item: Molina L
  item: Surinya KH
  item: Soos MA

Dimerization-induced activation of soluble insulin/IGF-1 receptor kinases: an alternative mechanism of activation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11714281
journal: Biochemistry
volume: 40
pages: 14268-78
published year: 2001
authors:
  item: Baer K
  item: Al-Hasani H
  item: Parvaresch S
  item: Corona T
  item: Rufer A
  item: Nolle V
  item: Bergschneider E
  item: Klein HW

Surfing the insulin signaling web.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11737239
journal: Eur J Clin Invest
volume: 31
pages: 966-77
published year: 2001
authors:
  item: Van Obberghen E
  item: Baron V
  item: Delahaye L
  item: Emanuelli B
  item: Filippa N
  item: Giorgetti-Peraldi S
  item: Lebrun P
  item: Mothe-Satney I
  item: Peraldi P
  item: Rocchi S
  item: Sawka-Verhelle D
  item: Tartare-Deckert S
  item: Giudicelli J

A PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11445579
journal: J Biol Chem
volume: 276
pages: 33419-27
published year: 2001
authors:
  item: Ligensa T
  item: Krauss S
  item: Demuth D
  item: Schumacher R
  item: Camonis J
  item: Jaques G
  item: Weidner KM

Cooperative regulation of the invasive and metastatic phenotypes by different domains of the type I insulin-like growth factor receptor beta subunit.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11445567
journal: J Biol Chem
volume: 276
pages: 33608-15
published year: 2001
authors:
  item: Brodt P
  item: Fallavollita L
  item: Khatib AM
  item: Samani AA
  item: Zhang D

Alanine scanning mutagenesis of a type 1 insulin-like growth factor receptor ligand binding site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11500492
journal: J Biol Chem
volume: 276
pages: 43980-6
published year: 2001
authors:
  item: Whittaker J
  item: Groth AV
  item: Mynarcik DC
  item: Pluzek L
  item: Gadsboll VL
  item: Whittaker LJ

The three dimensional structure of the type I insulin-like growth factor receptor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11376122
journal: Mol Pathol
volume: 54
pages: 125-32
published year: 2001
authors:
  item: Ward CW
  item: Garrett TP
  item: McKern NM
  item: Lou M
  item: Cosgrove LJ
  item: Sparrow LG
  item: Frenkel MJ
  item: Hoyne PA
  item: Elleman TC
  item: Adams TE
  item: Lovrecz GO
  item: Lawrence LJ
  item: Tulloch PA

Structure and autoregulation of the insulin-like growth factor 1 receptor kinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11694888
journal: Nat Struct Biol
volume: 8
pages: 1058-63
published year: 2001
authors:
  item: Favelyukis S
  item: Till JH
  item: Hubbard SR
  item: Miller WT
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure-function studies of an IGF-I analogue that can be chemically cleaved to a two-chain mini-IGF-I.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11287679
journal: Protein Eng
volume: 14
pages: 61-5
published year: 2001
authors:
  item: Geddes S
  item: Holst P
  item: Grotzinger J
  item: Gill R
  item: Nugent P
  item: De Meyts P
  item: Wollmer A
  item: Wood S
  item: Pitts J

Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11591350
journal: Structure (Camb)
volume: 9
pages: 955-65
published year: 2001
authors:
  item: Pautsch A
  item: Zoephel A
  item: Ahorn H
  item: Spevak W
  item: Hauptmann R
  item: Nar H
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12138114
journal: J Biol Chem
volume: 277
pages: 38797-802
published year: 2002
authors:
  item: Munshi S
  item: Kornienko M
  item: Hall DL
  item: Reid JC
  item: Waxman L
  item: Stirdivant SM
  item: Darke PL
  item: Kuo LC
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Cek3
type: KeggEnzyme

Cek5
type: KeggEnzyme

Cek6
type: KeggEnzyme

Cek7
type: KeggEnzyme

CFD1
type: KeggEnzyme

CKIT
type: KeggEnzyme

CSF1R
type: KeggEnzyme

DAlk
type: KeggEnzyme

DDR1
type: KeggEnzyme

DDR2
type: KeggEnzyme

Dek
type: KeggEnzyme

DKFZp434C1418
type: KeggEnzyme

Drosophila Eph kinase
type: KeggEnzyme

DRT
type: KeggEnzyme

DTK
type: KeggEnzyme

Ebk
type: KeggEnzyme

ECK
type: KeggEnzyme

EDDR1
type: KeggEnzyme

Eek
type: KeggEnzyme

EGFR
type: KeggEnzyme

Ehk2
type: KeggEnzyme

Ehk3
type: KeggEnzyme

Elk
type: KeggEnzyme

EPH
type: KeggEnzyme

EPHA1
type: KeggEnzyme

EPHA2
type: KeggEnzyme

EPHA6
type: KeggEnzyme

EPHA7
type: KeggEnzyme

EPHA8
type: KeggEnzyme

EPHB1
type: KeggEnzyme

EPHB2
type: KeggEnzyme

EPHB3
type: KeggEnzyme

EPHB4
type: KeggEnzyme

EphB5
type: KeggEnzyme

ephrin-B3 receptor tyrosine kinase
type: KeggEnzyme

EPHT
type: KeggEnzyme

EPHT2
type: KeggEnzyme

EPHT3
type: KeggEnzyme

EPHX
type: KeggEnzyme

ERBB
type: KeggEnzyme

ERBB1
type: KeggEnzyme

ERBB2
type: KeggEnzyme

ERBB3
type: KeggEnzyme

ERBB4
type: KeggEnzyme

ERK
type: KeggEnzyme

Eyk
type: KeggEnzyme

FGFR1
type: KeggEnzyme

FGFR2
type: KeggEnzyme

FGFR3
type: KeggEnzyme

FGFR4
type: KeggEnzyme

FLG
type: KeggEnzyme

FLK1
type: KeggEnzyme

FLK2
type: KeggEnzyme

FLT1
type: KeggEnzyme

FLT2
type: KeggEnzyme

FLT3
type: KeggEnzyme

FLT4
type: KeggEnzyme

FMS
type: KeggEnzyme

Fv2
type: KeggEnzyme

HBGFR
type: KeggEnzyme

HEK11
type: KeggEnzyme

HEK2
type: KeggEnzyme

HEK3
type: KeggEnzyme

HEK5
type: KeggEnzyme

HEK6
type: KeggEnzyme

HEP
type: KeggEnzyme

HER2
type: KeggEnzyme

HER3
type: KeggEnzyme

HER4
type: KeggEnzyme

HGFR
type: KeggEnzyme

HSCR1
type: KeggEnzyme

HTK
type: KeggEnzyme

IGF1R
type: KeggEnzyme

INSR
type: KeggEnzyme

INSRR
type: KeggEnzyme

insulin receptor protein-tyrosine kinase
type: KeggEnzyme

IR
type: KeggEnzyme

IRR
type: KeggEnzyme

JTK12
type: KeggEnzyme

JTK13
type: KeggEnzyme

JTK14
type: KeggEnzyme

JWS
type: KeggEnzyme

K-SAM
type: KeggEnzyme

KDR
type: KeggEnzyme

KGFR
type: KeggEnzyme

KIA0641
type: KeggEnzyme

KIAA1079
type: KeggEnzyme

KIAA1459
type: KeggEnzyme

Kil
type: KeggEnzyme

Kin15
type: KeggEnzyme

Kin16
type: KeggEnzyme

KIT
type: KeggEnzyme

KLG
type: KeggEnzyme

LTK
type: KeggEnzyme

MCF3
type: KeggEnzyme

Mdk1
type: KeggEnzyme

Mdk2
type: KeggEnzyme

Mdk5
type: KeggEnzyme

MEhk1
type: KeggEnzyme

MEN2A/B
type: KeggEnzyme

Mep
type: KeggEnzyme

MER
type: KeggEnzyme

MERTK
type: KeggEnzyme

MET
type: KeggEnzyme

Mlk1
type: KeggEnzyme

Mlk2
type: KeggEnzyme

Mrk
type: KeggEnzyme

MST1R
type: KeggEnzyme

MTC1
type: KeggEnzyme

MUSK
type: KeggEnzyme

Myk1
type: KeggEnzyme

N-SAM
type: KeggEnzyme

NEP
type: KeggEnzyme

NET
type: KeggEnzyme

Neu
type: KeggEnzyme

neurite outgrowth regulating kinase
type: KeggEnzyme

NGL
type: KeggEnzyme

NOK
type: KeggEnzyme

nork
type: KeggEnzyme

novel oncogene with kinase-domain
type: KeggEnzyme

Nsk2
type: KeggEnzyme

NTRK1
type: KeggEnzyme

NTRK2
type: KeggEnzyme

NTRK3
type: KeggEnzyme

NTRK4
type: KeggEnzyme

NTRKR1
type: KeggEnzyme

NTRKR2
type: KeggEnzyme

NTRKR3
type: KeggEnzyme

Nuk
type: KeggEnzyme

NYK
type: KeggEnzyme

PCL
type: KeggEnzyme

PDGFR
type: KeggEnzyme

PDGFRA
type: KeggEnzyme

PDGFRB
type: KeggEnzyme

PHB6
type: KeggEnzyme

protein-tyrosine kinase (ambiguous)
type: KeggEnzyme

protein tyrosine kinase (ambiguous)
type: KeggEnzyme

PTK
type: KeggEnzyme

PTK3
type: KeggEnzyme

PTK7
type: KeggEnzyme

receptor protein tyrosine kinase
type: KeggEnzyme

RET
type: KeggEnzyme

RON
type: KeggEnzyme

ROR1
type: KeggEnzyme

ROR2
type: KeggEnzyme

ROS1
type: KeggEnzyme

RSE
type: KeggEnzyme

RTK
type: KeggEnzyme

RYK
type: KeggEnzyme

SEA
type: KeggEnzyme

Sek2
type: KeggEnzyme

Sek3
type: KeggEnzyme

Sek4
type: KeggEnzyme

Sfr
type: KeggEnzyme

SKY
type: KeggEnzyme

STK
type: KeggEnzyme

STK1
type: KeggEnzyme

TEK
type: KeggEnzyme

TIE
type: KeggEnzyme

TIE1
type: KeggEnzyme

TIE2
type: KeggEnzyme

TIF
type: KeggEnzyme

TKT
type: KeggEnzyme

TRK
type: KeggEnzyme

TRKA
type: KeggEnzyme

TRKB
type: KeggEnzyme

TRKC
type: KeggEnzyme

TRKE
type: KeggEnzyme

TYK1
type: KeggEnzyme

TYRO10
type: KeggEnzyme

Tyro11
type: KeggEnzyme

TYRO3
type: KeggEnzyme

Tyro5
type: KeggEnzyme

Tyro6
type: KeggEnzyme

TYRO7
type: KeggEnzyme

UFO
type: KeggEnzyme

VEGFR1
type: KeggEnzyme

VEGFR2
type: KeggEnzyme

VEGFR3
type: KeggEnzyme

Vik
type: KeggEnzyme

YK1
type: KeggEnzyme

Yrk
type: KeggEnzyme

Analogue
compound: ATP
pdb: 1jqhA01
ligand het code: ANP

Analogue
compound: ATP
pdb: 1jqhB01
ligand het code: ANP

Analogue
compound: ATP
pdb: 1jqhC01
ligand het code: ANP

Analogue
compound: ATP
pdb: 1k3aA01
ligand het code: ACP

ReferenceForCatalyticMechanism
reference index: 17
reference section: p.10061

ReferenceForCatalyticMechanism
reference index: 19
reference section: p.959