Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2BZN

Crystal structure of human guanosine monophosphate reductase 2 GMPR2 in complex with IMP

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
E0003824molecular_functioncatalytic activity
E0003920molecular_functionGMP reductase activity
E0005515molecular_functionprotein binding
E0005829cellular_componentcytosol
E0006144biological_processpurine nucleobase metabolic process
E0006163biological_processpurine nucleotide metabolic process
E0009117biological_processnucleotide metabolic process
E0016491molecular_functionoxidoreductase activity
E0046037biological_processGMP metabolic process
E0046872molecular_functionmetal ion binding
E1902560cellular_componentGMP reductase complex
F0003824molecular_functioncatalytic activity
F0003920molecular_functionGMP reductase activity
F0005515molecular_functionprotein binding
F0005829cellular_componentcytosol
F0006144biological_processpurine nucleobase metabolic process
F0006163biological_processpurine nucleotide metabolic process
F0009117biological_processnucleotide metabolic process
F0016491molecular_functionoxidoreductase activity
F0046037biological_processGMP metabolic process
F0046872molecular_functionmetal ion binding
F1902560cellular_componentGMP reductase complex
G0003824molecular_functioncatalytic activity
G0003920molecular_functionGMP reductase activity
G0005515molecular_functionprotein binding
G0005829cellular_componentcytosol
G0006144biological_processpurine nucleobase metabolic process
G0006163biological_processpurine nucleotide metabolic process
G0009117biological_processnucleotide metabolic process
G0016491molecular_functionoxidoreductase activity
G0046037biological_processGMP metabolic process
G0046872molecular_functionmetal ion binding
G1902560cellular_componentGMP reductase complex
H0003824molecular_functioncatalytic activity
H0003920molecular_functionGMP reductase activity
H0005515molecular_functionprotein binding
H0005829cellular_componentcytosol
H0006144biological_processpurine nucleobase metabolic process
H0006163biological_processpurine nucleotide metabolic process
H0009117biological_processnucleotide metabolic process
H0016491molecular_functionoxidoreductase activity
H0046037biological_processGMP metabolic process
H0046872molecular_functionmetal ion binding
H1902560cellular_componentGMP reductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE IMP A 1338
ChainResidue
AALA53
AGLY242
AGLY243
AGLY268
AMET269
ASER270
AGLU289
AGLY290
AHOH2142
AHOH2216
AHOH2217
AMET55
AHOH2218
AHOH2219
AGLY183
ASER184
ACYS186
AASP219
AGLY220
AGLY221
AMET240

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE IMP B 1338
ChainResidue
BALA53
BMET55
BGLY183
BSER184
BCYS186
BASP219
BGLY220
BGLY221
BMET240
BGLY242
BGLY243
BGLY268
BMET269
BSER270
BGLU289
BGLY290
BHOH2036
BHOH2204
BHOH2207
BHOH2209
BHOH2210
BHOH2211

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE IMP C 1338
ChainResidue
CALA53
CMET55
CGLY183
CSER184
CCYS186
CASP219
CGLY220
CGLY221
CMET240
CGLY242
CGLY243
CGLY268
CMET269
CSER270
CGLU289
CGLY290
CHOH2047
CHOH2160
CHOH2173
CHOH2263
CHOH2264
CHOH2265
CHOH2266
CHOH2267

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE IMP D 1338
ChainResidue
DALA53
DMET55
DGLY183
DSER184
DCYS186
DASP219
DGLY220
DGLY221
DMET240
DGLY242
DGLY243
DGLY268
DMET269
DSER270
DGLU289
DGLY290
DHOH2153
DHOH2221
DHOH2222
DHOH2224
DHOH2225
DHOH2226

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE IMP E 1338
ChainResidue
EGLY243
EGLY268
EMET269
ESER270
EGLU289
EGLY290
EHOH2053
EHOH2169
EHOH2279
EHOH2280
EHOH2281
EHOH2282
EHOH2283
EALA53
EMET55
EGLY183
ESER184
ECYS186
EASP219
EGLY220
EGLY221
EMET240
EGLY242

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE IMP F 1338
ChainResidue
FALA53
FASN158
FGLY183
FSER184
FCYS186
FASP219
FGLY220
FGLY221
FMET240
FGLY242
FGLY243
FGLY268
FMET269
FSER270
FGLU289
FGLY290
FHOH2052
FHOH2171
FHOH2254
FHOH2255
FHOH2256
FHOH2257

site_idAC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE IMP G 1338
ChainResidue
GALA53
GMET55
GGLY183
GSER184
GCYS186
GASP219
GGLY220
GGLY221
GMET240
GGLY242
GGLY243
GGLY268
GMET269
GSER270
GGLU289
GGLY290
GHOH2111
GHOH2124
GHOH2127
GHOH2193
GHOH2194
GHOH2195
GHOH2196
GHOH2197
GHOH2198

site_idAC8
Number of Residues23
DetailsBINDING SITE FOR RESIDUE IMP H 1338
ChainResidue
HALA53
HMET55
HGLY183
HSER184
HCYS186
HASP219
HGLY220
HGLY221
HMET240
HGLY242
HGLY243
HGLY268
HMET269
HSER270
HGLU289
HGLY290
HHOH2047
HHOH2145
HHOH2244
HHOH2247
HHOH2248
HHOH2249
HHOH2250

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 Residues8
DetailsActive site: {"description":"Thioimidate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
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 Residues40
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 Residues72
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon