DB code: S00382
| CATH domain | 3.40.50.9100 : Rossmann fold | Catalytic domain |
|---|---|---|
| E.C. | 4.2.1.10 | |
| CSA | ||
| M-CSA | ||
| MACiE | M0055 | |
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P15474 |
3-dehydroquinate dehydratase
|
3-dehydroquinase
EC 4.2.1.10 Type II DHQase |
NP_626225.1
(Protein)
NC_003888.3 (DNA/RNA sequence) |
PF01220
(DHquinase_II)
[Graphical View] |
| P0A4Z6 |
3-dehydroquinate dehydratase
|
3-dehydroquinase
EC 4.2.1.10 Type II DHQase |
NP_217053.1
(Protein)
NC_000962.3 (DNA/RNA sequence) NP_337108.1 (Protein) NC_002755.2 (DNA/RNA sequence) YP_006515978.1 (Protein) NC_018143.1 (DNA/RNA sequence) |
PF01220
(DHquinase_II)
[Graphical View] |
| P54517 |
3-dehydroquinate dehydratase
|
3-dehydroquinase
EC 4.2.1.10 Type II DHQase |
NP_390327.1
(Protein)
NC_000964.3 (DNA/RNA sequence) |
PF01220
(DHquinase_II)
[Graphical View] |
| KEGG enzyme name |
|---|
|
3-dehydroquinate dehydratase
3-dehydroquinate hydrolase DHQase dehydroquinate dehydratase 3-dehydroquinase 5-dehydroquinase dehydroquinase 5-dehydroquinate dehydratase 5-dehydroquinate hydro-lyase 3-dehydroquinate hydro-lyase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P15474 | AROQ_STRCO | 3-dehydroquinate = 3-dehydroshikimate + H(2)O. | Homododecamer. | ||
| P0A4Z6 | AROQ_MYCTU | 3-dehydroquinate = 3-dehydroshikimate + H(2)O. | Homododecamer. | ||
| P54517 | AROQ_BACSU | 3-dehydroquinate = 3-dehydroshikimate + H(2)O. | Homododecamer. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00400 | Phenylalanine, tyrosine and tryptophan biosynthesis |
| Compound table | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||
| KEGG-id | C00944 | C02637 | C00001 | ||||||
| E.C. | |||||||||
| Compound | 3-Dehydroquinate | 3-Dehydroshikimate | H2O | ||||||
| Type | carbohydrate,carboxyl group | carbohydrate,carboxyl group | H2O | ||||||
| ChEBI |
17947 17947 |
30918 30918 |
15377 15377 |
||||||
| PubChem |
439351 439351 |
439774 439774 |
22247451 962 22247451 962 |
||||||
| 1d0iA |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iB |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iC |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iD |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iE |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iF |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iG |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iH |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iI |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iJ |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iK |
|
|
|
|
|
Unbound | Unbound | ||
| 1d0iL |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0A |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0B |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0C |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0D |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0E |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0F |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0G |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0H |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0I |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0J |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0K |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu0L |
|
|
|
|
|
Unbound | Unbound | ||
| 1gu1A |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1B |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1C |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1D |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1E |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1F |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1G |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1H |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1I |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1J |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1K |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gu1L |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1gtzA |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzB |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzC |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzD |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzE |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzF |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzG |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzH |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzI |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzJ |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzK |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1gtzL |
|
|
|
|
|
Unbound | Bound:DHK | ||
| 1h05A |
|
|
|
|
|
Unbound | Unbound | ||
| 1h0rA |
|
|
|
|
|
Analogue:FA1 | Unbound | ||
| 1h0sA |
|
|
|
|
|
Analogue:FA6 | Unbound | ||
| 2dhqA |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoA |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoB |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoC |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoD |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoE |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoF |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoG |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoH |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoI |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoJ |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoK |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoL |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoM |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoN |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoO |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoP |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoQ |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoR |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoS |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoT |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoU |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoV |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoX |
|
|
|
|
|
Unbound | Unbound | ||
| 1gqoY |
|
|
|
|
|
Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature [4] & [12] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1d0iA |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iB |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iC |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iD |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iE |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iF |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iG |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iH |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iI |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iJ |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iK |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1d0iL |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0A |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0B |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0C |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0D |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0E |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0F |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0G |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0H |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0I |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0J |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0K |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu0L |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1A |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1B |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1C |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1D |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1E |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1F |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1G |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1H |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1I |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1J |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1K |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gu1L |
|
|
|
|
|
ASN 16;ARG 23;TYR 28;HIS 106 | ||||
| 1gtzA |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzB |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzC |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzD |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzE |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzF |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzG |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzH |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzI |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzJ |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzK |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1gtzL |
|
|
|
|
|
ASN 16; ;TYR 28;HIS 106 | mutant R23A | |||
| 1h05A |
|
|
|
|
|
ASN 12;ARG 19; ;HIS 101 | invisible 24Y | |||
| 1h0rA |
|
|
|
|
|
ASN 12; ;TYR 24;HIS 101 | invisible 19R | |||
| 1h0sA |
|
|
|
|
|
ASN 12;ARG 19; ;HIS 101 | invisible 24Y | |||
| 2dhqA |
|
|
|
|
|
ASN 12;ARG 19; ;HIS 101 | invisible 24Y | |||
| 1gqoA |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoB |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoC |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoD |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoE |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoF |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoG |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoH |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoI |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoJ |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoK |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoL |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoM |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoN |
|
|
|
|
|
ASN 10; ; ;HIS 99 | invisible 16-24 | |||
| 1gqoO |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoP |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoQ |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoR |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoS |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoT |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoU |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| 1gqoV |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | invisible 18-23 | |||
| 1gqoX |
|
|
|
|
|
ASN 10; ; ;HIS 99 | invisible 17-23 | |||
| 1gqoY |
|
|
|
|
|
ASN 10;ARG 17; ;HIS 99 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[8]
|
Fig. 1, p.522 | 3 |
|
[12]
|
Fig.8, p.497-498 | 2 |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1554351 |
| Journal | Biochem J |
| Year | 1992 |
| Volume | 282 |
| Pages | 687-95 |
| Authors | Kleanthous C, Deka R, Davis K, Kelly SM, Cooper A, Harding SE, Price NC, Hawkins AR, Coggins JR |
| Title | A comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymes. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8064862 |
| Journal | J Mol Biol |
| Year | 1994 |
| Volume | 241 |
| Pages | 488-91 |
| Authors | Gourley DG, Coggins JR, Isaacs NW, Moore JD, Charles IG, Hawkins AR |
| Title | Crystallization of a type II dehydroquinase from Mycobacterium tuberculosis. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8870678 |
| Journal | Biochem J |
| Year | 1996 |
| Volume | 319 |
| Pages | 269-78 |
| Authors | Bottomley JR, Hawkins AR, Kleanthous C |
| Title | Conformational changes and the role of metals in the mechanism of type II dehydroquinase from Aspergillus nidulans. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8798709 |
| Journal | J Biol Chem |
| Year | 1996 |
| Volume | 271 |
| Pages | 24492-7 |
| Authors | Krell T, Horsburgh MJ, Cooper A, Kelly SM, Coggins JR |
| Title |
Localization of the active site of type II dehydroquinases. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9147947 |
| Journal | Biochem Soc Trans |
| Year | 1997 |
| Volume | 25 |
| Pages | 348; replaces 93S |
| Authors | Boam DJ, Price NC, Kelly SM, Krell T, Coggins JR |
| Title | Evidence that the active site in type II dehydroquinase from Streptomyces coelicolor is near the single tryptophan. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9473305 |
| Journal | Arch Biochem Biophys |
| Year | 1998 |
| Volume | 350 |
| Pages | 298-306 |
| Authors | Florova G, Denoya CD, Morgenstern MR, Skinner DD, Reynolds KA |
| Title |
Cloning, |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9931316 |
| Journal | Biochem J |
| Year | 1999 |
| Volume | 338 |
| Pages | 195-202 |
| Authors | Price NC, Boam DJ, Kelly SM, Duncan D, Krell T, Gourley DG, Coggins JR, Virden R, Hawkins AR |
| Title | The folding and assembly of the dodecameric type II dehydroquinases. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10360352 |
| Journal | Nat Struct Biol |
| Year | 1999 |
| Volume | 6 |
| Pages | 521-5 |
| Authors | Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L |
| Title | The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction. |
| Related PDB | 2dhq |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10698442 |
| Journal | Bioorg Med Chem Lett |
| Year | 2000 |
| Volume | 10 |
| Pages | 231-4 |
| Authors | Parker EJ, Gonzalez Bello C, Coggins JR, Hawkins AR, Abell C |
| Title | Mechanistic studies on type I and type II dehydroquinase with (6R)- and (6S)-6-fluoro-3-dehydroquinic acids. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11173479 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2001 |
| Volume | 57 |
| Pages | 279-80 |
| Authors | Kwak JE, Lee JY, Han BW, Moon J J, Sohn SH, Suh SW |
| Title | Crystallization and preliminary X-ray crystallographic analysis of type II dehydroquinase from Helicobacter pylori. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12387860 |
| Journal | FEBS Lett |
| Year | 2002 |
| Volume | 530 |
| Pages | 24-30 |
| Authors | Evans LD, Roszak AW, Noble LJ, Robinson DA, Chalk PA, Matthews JL, Coggins JR, Price NC, Lapthorn AJ |
| Title | Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions. |
| Related PDB | 1h05 |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 11937054 |
| Journal | Structure (Camb) |
| Year | 2002 |
| Volume | 10 |
| Pages | 493-503 |
| Authors | Roszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ |
| Title | The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor. |
| Related PDB | 1d0i 1gu0 1gu1 1gtz |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12784220 |
| Journal | Proteins |
| Year | 2003 |
| Volume | 51 |
| Pages | 616-7 |
| Authors | Lee BI, Kwak JE, Suh SW |
| Title | Crystal structure of the type II 3-dehydroquinase from Helicobacter pylori. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
| Created | Updated |
|---|---|
| 2004-04-10 | 2009-02-26 |