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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
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03195
ChainResidueDetails
DCYS186
ACYS186
BCYS186
CCYS186

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_03195
ChainResidueDetails
DTHR188
ATHR188
BTHR188
CTHR188

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469
ChainResidueDetails
CSER26
CSER314
DSER26
DSER314
ASER26
ASER314
BSER26
BSER314

site_idSWS_FT_FI4
Number of Residues20
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:22037469
ChainResidueDetails
ATYR285
BLYS78
BASP129
BILE180
BMET269
BTYR285
CLYS78
CASP129
CILE180
CMET269
CTYR285
DLYS78
DASP129
DILE180
DMET269
DTYR285
ALYS78
AASP129
AILE180
AMET269

site_idSWS_FT_FI5
Number of Residues32
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03195
ChainResidueDetails
AGLY181
AGLY183
ACYS186
BASP219
BGLY242
BGLY268
BARG286
CGLY181
CGLY183
CCYS186
CARG189
CASP219
CGLY242
CGLY268
CARG286
DGLY181
DGLY183
DCYS186
DARG189
DASP219
DGLY242
DGLY268
DARG286
AARG189
AASP219
AGLY242
AGLY268
AARG286
BGLY181
BGLY183
BCYS186
BARG189

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS291
BLYS291
CLYS291
DLYS291

219869

PDB entries from 2024-05-15

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