4RC9

Crystal Structure of the type II Dehydroquinate dehydratase from Acinetobacter baumannii at 2.03A Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003855	molecular_function	3-dehydroquinate dehydratase activity
A	0009423	biological_process	chorismate biosynthetic process
A	0019631	biological_process	quinate catabolic process
B	0003855	molecular_function	3-dehydroquinate dehydratase activity
B	0009423	biological_process	chorismate biosynthetic process
B	0019631	biological_process	quinate catabolic process
C	0003855	molecular_function	3-dehydroquinate dehydratase activity
C	0009423	biological_process	chorismate biosynthetic process
C	0019631	biological_process	quinate catabolic process
D	0003855	molecular_function	3-dehydroquinate dehydratase activity
D	0009423	biological_process	chorismate biosynthetic process
D	0019631	biological_process	quinate catabolic process
E	0003855	molecular_function	3-dehydroquinate dehydratase activity
E	0009423	biological_process	chorismate biosynthetic process
E	0019631	biological_process	quinate catabolic process
F	0003855	molecular_function	3-dehydroquinate dehydratase activity
F	0009423	biological_process	chorismate biosynthetic process
F	0019631	biological_process	quinate catabolic process
G	0003855	molecular_function	3-dehydroquinate dehydratase activity
G	0009423	biological_process	chorismate biosynthetic process
G	0019631	biological_process	quinate catabolic process
H	0003855	molecular_function	3-dehydroquinate dehydratase activity
H	0009423	biological_process	chorismate biosynthetic process
H	0019631	biological_process	quinate catabolic process
I	0003855	molecular_function	3-dehydroquinate dehydratase activity
I	0009423	biological_process	chorismate biosynthetic process
I	0019631	biological_process	quinate catabolic process
J	0003855	molecular_function	3-dehydroquinate dehydratase activity
J	0009423	biological_process	chorismate biosynthetic process
J	0019631	biological_process	quinate catabolic process
K	0003855	molecular_function	3-dehydroquinate dehydratase activity
K	0009423	biological_process	chorismate biosynthetic process
K	0019631	biological_process	quinate catabolic process
L	0003855	molecular_function	3-dehydroquinate dehydratase activity
L	0009423	biological_process	chorismate biosynthetic process
L	0019631	biological_process	quinate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 201

Chain	Residue
A	ASN76
A	HIS102
A	LEU103
A	SER104
A	HOH322
A	HOH345

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 201

Chain	Residue
B	SER104
B	HOH302
B	ASN76
B	HIS102
B	LEU103

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 201

Chain	Residue
C	ASN76
C	HIS102
C	LEU103
C	SER104
C	HOH353

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 201

Chain	Residue
D	ASN76
D	HIS102
D	LEU103
D	SER104
D	HOH309

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 201

Chain	Residue
E	ASN76
E	ALA78
E	HIS102
E	LEU103
E	SER104
E	HOH353

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 F 201

Chain	Residue
F	ASN76
F	ALA78
F	HIS102
F	LEU103
F	SER104
F	HOH326
F	HOH327

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 G 201

Chain	Residue
G	ASN76
G	ALA78
G	HIS102
G	LEU103
G	SER104
G	HOH340

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 H 201

Chain	Residue
H	ASN76
H	HIS102
H	LEU103
H	SER104

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 I 201

Chain	Residue
I	ASN76
I	HIS102
I	LEU103
I	SER104
I	HOH337

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 J 201

Chain	Residue
J	ASN76
J	HIS102
J	LEU103
J	SER104
J	HOH301
J	HOH312

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 K 201

Chain	Residue
K	ASN76
K	HIS102
K	LEU103
K	SER104
K	HOH310

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 L 201

Chain	Residue
L	ASN76
L	ALA78
L	HIS102
L	LEU103
L	SER104
L	HOH338

---

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	12
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---