5YDB

Crystal structure of the complex of type II dehydroquinate dehydratase from Acinetobacter baumannii with dehydroquinic acid at 1.76 Angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003855	molecular_function	3-dehydroquinate dehydratase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009073	biological_process	aromatic amino acid family biosynthetic process
A	0009423	biological_process	chorismate biosynthetic process
A	0016829	molecular_function	lyase activity
A	0019631	biological_process	quinate catabolic process
B	0003855	molecular_function	3-dehydroquinate dehydratase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009073	biological_process	aromatic amino acid family biosynthetic process
B	0009423	biological_process	chorismate biosynthetic process
B	0016829	molecular_function	lyase activity
B	0019631	biological_process	quinate catabolic process
C	0003855	molecular_function	3-dehydroquinate dehydratase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0009073	biological_process	aromatic amino acid family biosynthetic process
C	0009423	biological_process	chorismate biosynthetic process
C	0016829	molecular_function	lyase activity
C	0019631	biological_process	quinate catabolic process
D	0003855	molecular_function	3-dehydroquinate dehydratase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0009073	biological_process	aromatic amino acid family biosynthetic process
D	0009423	biological_process	chorismate biosynthetic process
D	0016829	molecular_function	lyase activity
D	0019631	biological_process	quinate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue NA A 201

Chain	Residue
A	HIS107
A	CYS127

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site_id	AC2
Number of Residues	10
Details	binding site for residue DQA A 202

Chain	Residue
A	SER104
A	ARG113
A	HOH310
A	ASN76
A	ALA78
A	ALA79
A	HIS82
A	ASP89
A	HIS102
A	LEU103

---

site_id	AC3
Number of Residues	2
Details	binding site for residue NA B 201

Chain	Residue
B	HIS107
B	CYS127

---

site_id	AC4
Number of Residues	10
Details	binding site for residue DQA B 202

Chain	Residue
B	ASN76
B	ALA78
B	ALA79
B	HIS82
B	HIS102
B	LEU103
B	SER104
B	ARG113
B	HOH324
D	ASP89

---

site_id	AC5
Number of Residues	2
Details	binding site for residue NA C 201

Chain	Residue
C	HIS107
C	CYS127

---

site_id	AC6
Number of Residues	11
Details	binding site for residue DQA C 202

Chain	Residue
B	ASP89
C	ASN76
C	ALA78
C	ALA79
C	HIS82
C	HIS102
C	LEU103
C	SER104
C	VAL106
C	ARG113
C	HOH309

---

site_id	AC7
Number of Residues	2
Details	binding site for residue NA D 201

Chain	Residue
D	HIS107
D	CYS127

---

site_id	AC8
Number of Residues	11
Details	binding site for residue DQA D 202

Chain	Residue
C	ASP89
D	ASN76
D	ALA78
D	ALA79
D	HIS82
D	HIS102
D	LEU103
D	SER104
D	ARG109
D	ARG113
D	HOH313

---

Functional Information from PROSITE/UniProt

site_id	PS01029
Number of Residues	18
Details	DEHYDROQUINASE_II Dehydroquinase class II signature. IHGPNLnlLGkREpevYG

Chain	Residue	Details
A	ILE8-GLY25

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00169

Chain	Residue	Details
A	TYR24
B	TYR24
C	TYR24
D	TYR24

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00169

Chain	Residue	Details
A	HIS102
B	HIS102
C	HIS102
D	HIS102

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00169

Chain	Residue	Details
A	ASN76
B	ARG113
C	ASN76
C	HIS82
C	ASP89
C	LEU103
C	ARG113
D	ASN76
D	HIS82
D	ASP89
D	LEU103
A	HIS82
D	ARG113
A	ASP89
A	LEU103
A	ARG113
B	ASN76
B	HIS82
B	ASP89
B	LEU103

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00169

Chain	Residue	Details
A	ARG19
B	ARG19
C	ARG19
D	ARG19

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