6HSU

The crystal structure of type II Dehydroquinase from Psychromonas ingrahamii 37, crystal form 2

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	9
Details	binding site for residue TLA A 201

Chain	Residue
A	ASN77
A	ALA79
A	HIS83
A	HIS103
A	LEU104
A	SER105
A	ARG110
A	ARG114
A	HOH330

---

site_id	AC2
Number of Residues	10
Details	binding site for residue TLA B 201

Chain	Residue
B	ASN77
B	ALA79
B	ALA80
B	HIS83
B	HIS103
B	LEU104
B	SER105
B	ARG114
B	HOH315
B	HOH319

---

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL B 202

Chain	Residue
B	ASP40
B	GLU41
B	LEU44
B	HOH308
B	HOH333
K	HIS0
K	ASN46

---

site_id	AC4
Number of Residues	9
Details	binding site for residue TLA C 201

Chain	Residue
C	ASN77
C	ALA79
C	ALA80
C	HIS83
C	HIS103
C	LEU104
C	SER105
C	ARG114
C	HOH320

---

site_id	AC5
Number of Residues	11
Details	binding site for residue TLA D 201

Chain	Residue
D	ASN77
D	ALA79
D	ALA80
D	THR82
D	HIS83
D	HIS103
D	LEU104
D	SER105
D	ARG114
D	HOH336
D	HOH350

---

site_id	AC6
Number of Residues	10
Details	binding site for residue TLA E 201

Chain	Residue
E	ASN77
E	ALA79
E	ALA80
E	HIS83
E	HIS103
E	LEU104
E	SER105
E	ARG110
E	ARG114
E	HOH325

---

site_id	AC7
Number of Residues	10
Details	binding site for residue TLA F 201

Chain	Residue
F	ASN77
F	ALA79
F	ALA80
F	HIS83
F	HIS103
F	LEU104
F	SER105
F	VAL107
F	ARG114
F	HOH312

---

site_id	AC8
Number of Residues	9
Details	binding site for residue TLA G 201

Chain	Residue
G	ASN77
G	ALA79
G	ALA80
G	HIS83
G	HIS103
G	LEU104
G	SER105
G	VAL107
G	ARG114

---

site_id	AC9
Number of Residues	9
Details	binding site for residue TLA H 201

Chain	Residue
H	ASN77
H	ALA79
H	ALA80
H	HIS83
H	HIS103
H	LEU104
H	SER105
H	ARG114
H	HOH336

---

site_id	AD1
Number of Residues	10
Details	binding site for residue TLA I 201

Chain	Residue
I	ASN77
I	ALA79
I	ALA80
I	HIS83
I	HIS103
I	LEU104
I	SER105
I	VAL107
I	ARG114
I	HOH319

---

site_id	AD2
Number of Residues	11
Details	binding site for residue TLA J 201

Chain	Residue
J	HIS103
J	LEU104
J	SER105
J	ARG114
J	HOH330
J	HOH337
J	ASN77
J	ALA79
J	ALA80
J	THR82
J	HIS83

---

site_id	AD3
Number of Residues	9
Details	binding site for residue TLA K 201

Chain	Residue
K	ASN77
K	ALA79
K	ALA80
K	HIS83
K	HIS103
K	LEU104
K	SER105
K	VAL107
K	ARG114

---

site_id	AD4
Number of Residues	4
Details	binding site for residue MPO K 202

Chain	Residue
K	GLN3
K	GLU69
K	LYS70
K	ASP72

---

site_id	AD5
Number of Residues	10
Details	binding site for residue TLA L 201

Chain	Residue
L	ASN77
L	ALA79
L	ALA80
L	HIS83
L	HIS103
L	LEU104
L	SER105
L	VAL107
L	ARG114
L	HOH340

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU10-GLY27

---

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

---