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2A7R

Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003920molecular_functionGMP reductase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006144biological_processpurine nucleobase metabolic process
A0006163biological_processpurine nucleotide metabolic process
A0009117biological_processnucleotide metabolic process
A0016491molecular_functionoxidoreductase activity
A0046037biological_processGMP metabolic process
A0046872molecular_functionmetal ion binding
A1902560cellular_componentGMP reductase complex
B0003824molecular_functioncatalytic activity
B0003920molecular_functionGMP reductase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006144biological_processpurine nucleobase metabolic process
B0006163biological_processpurine nucleotide metabolic process
B0009117biological_processnucleotide metabolic process
B0016491molecular_functionoxidoreductase activity
B0046037biological_processGMP metabolic process
B0046872molecular_functionmetal ion binding
B1902560cellular_componentGMP reductase complex
C0003824molecular_functioncatalytic activity
C0003920molecular_functionGMP reductase activity
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0006144biological_processpurine nucleobase metabolic process
C0006163biological_processpurine nucleotide metabolic process
C0009117biological_processnucleotide metabolic process
C0016491molecular_functionoxidoreductase activity
C0046037biological_processGMP metabolic process
C0046872molecular_functionmetal ion binding
C1902560cellular_componentGMP reductase complex
D0003824molecular_functioncatalytic activity
D0003920molecular_functionGMP reductase activity
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0006144biological_processpurine nucleobase metabolic process
D0006163biological_processpurine nucleotide metabolic process
D0009117biological_processnucleotide metabolic process
D0016491molecular_functionoxidoreductase activity
D0046037biological_processGMP metabolic process
D0046872molecular_functionmetal ion binding
D1902560cellular_componentGMP reductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
ATHR33
AARG34
ASER35
ALYS325

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
APHE149
APRO150
AGLN151
AHIS152

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1400
ChainResidue
BARG34
BSER35
BLYS323
BLYS325
BTHR33

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1401
ChainResidue
BPHE149
BPRO150
BGLN151
BHIS152

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 2400
ChainResidue
CTHR33
CARG34
CSER35

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 2401
ChainResidue
CPHE149
CPRO150
CGLN151
CHIS152

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 3400
ChainResidue
DTHR33
DARG34
DSER35
DLYS325

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 3500
ChainResidue
DGLY183
DSER184
DGLY220
DGLY221
DCYS222
DGLY242
DGLY243

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 5GP A 500
ChainResidue
AMET55
AGLY183
ASER184
ACYS186
ATHR188
AASP219
AGLY220
AGLY221
AGLY242
AGLY243
AGLY268
AMET269
ASER270
AARG286
AALA287
ASER288
AGLY290

site_idBC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 5GP B 500
ChainResidue
BALA53
BMET55
BGLY183
BSER184
BCYS186
BTHR188
BASP219
BGLY220
BGLY221
BGLY242
BGLY243
BGLY268
BSER270
BARG286
BSER288
BGLY290

site_idBC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 5GP C 500
ChainResidue
CALA53
CMET55
CSER184
CCYS186
CTHR188
CASP219
CGLY220
CGLY221
CGLY242
CGLY243
CGLY268
CMET269
CSER270
CGLY290

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGIGpGSVCtT
ChainResidueDetails
AILE176-THR188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Thioimidate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22037469","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22037469","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues38
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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