2BWG

Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003920	molecular_function	GMP reductase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006144	biological_process	purine nucleobase metabolic process
A	0006163	biological_process	purine nucleotide metabolic process
A	0009117	biological_process	nucleotide metabolic process
A	0009409	biological_process	response to cold
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	1902560	cellular_component	GMP reductase complex
B	0003824	molecular_function	catalytic activity
B	0003920	molecular_function	GMP reductase activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006144	biological_process	purine nucleobase metabolic process
B	0006163	biological_process	purine nucleotide metabolic process
B	0009117	biological_process	nucleotide metabolic process
B	0009409	biological_process	response to cold
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	1902560	cellular_component	GMP reductase complex
C	0003824	molecular_function	catalytic activity
C	0003920	molecular_function	GMP reductase activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0006144	biological_process	purine nucleobase metabolic process
C	0006163	biological_process	purine nucleotide metabolic process
C	0009117	biological_process	nucleotide metabolic process
C	0009409	biological_process	response to cold
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	1902560	cellular_component	GMP reductase complex
D	0003824	molecular_function	catalytic activity
D	0003920	molecular_function	GMP reductase activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0006144	biological_process	purine nucleobase metabolic process
D	0006163	biological_process	purine nucleotide metabolic process
D	0009117	biological_process	nucleotide metabolic process
D	0009409	biological_process	response to cold
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	1902560	cellular_component	GMP reductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A1339

Chain	Residue
A	GLY181
A	PRO182
A	GLY183
A	CYS186
A	ARG189

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K B1338

Chain	Residue
B	GLY181
B	GLY183
B	CYS186

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K C1338

Chain	Residue
C	GLY183
C	CYS186
C	ARG189
C	GLY181

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D1338

Chain	Residue
D	GLY181
D	GLY183
D	CYS186
D	ARG189

---

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 5GP A1340

Chain	Residue
A	ALA53
A	MET55
A	GLY183
A	SER184
A	CYS186
A	ASP219
A	GLY220
A	GLY221
A	MET240
A	LEU241
A	GLY242
A	GLY243
A	GLY268
A	MET269
A	SER270
A	ARG286
A	ALA287
A	SER288
A	GLY290
A	HOH2009
A	HOH2046
A	HOH2058
A	HOH2059
A	HOH2060

---

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE 5GP B1339

Chain	Residue
B	ALA53
B	MET55
B	ASN158
B	GLY183
B	SER184
B	CYS186
B	ASP219
B	GLY220
B	GLY221
B	LEU241
B	GLY242
B	GLY243
B	GLY268
B	MET269
B	SER270
B	ARG286
B	ALA287
B	SER288
B	GLY290
B	HOH2010
B	HOH2036
B	HOH2049
B	HOH2050

---

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 5GP C1339

Chain	Residue
C	ALA53
C	MET55
C	ASN158
C	GLY183
C	SER184
C	CYS186
C	ASP219
C	GLY220
C	GLY221
C	MET240
C	GLY242
C	GLY243
C	GLY268
C	MET269
C	SER270
C	ARG286
C	SER288
C	GLY290
C	HOH2033
C	HOH2046
C	HOH2047

---

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 5GP D1339

Chain	Residue
D	ARG286
D	ALA287
D	SER288
D	GLY290
D	HOH2029
D	ALA53
D	MET55
D	ASN158
D	GLY183
D	SER184
D	CYS186
D	ASP219
D	GLY220
D	GLY221
D	LEU241
D	GLY242
D	GLY243
D	GLY268
D	MET269
D	SER270

---

Functional Information from PROSITE/UniProt

site_id	PS00487
Number of Residues	13
Details	IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGVGpGSVCtT

Chain	Residue	Details
A	ILE176-THR188

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Thioimidate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

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