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2VXO

Human GMP synthetase in complex with XMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003921molecular_functionGMP synthase activity
A0003922molecular_functionGMP synthase (glutamine-hydrolyzing) activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006541biological_processglutamine metabolic process
A0009113biological_processpurine nucleobase biosynthetic process
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0016874molecular_functionligase activity
A0046037biological_processGMP metabolic process
B0003921molecular_functionGMP synthase activity
B0003922molecular_functionGMP synthase (glutamine-hydrolyzing) activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006541biological_processglutamine metabolic process
B0009113biological_processpurine nucleobase biosynthetic process
B0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
B0016874molecular_functionligase activity
B0046037biological_processGMP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE XMP A 1694
ChainResidue
AARG337
ATHR689
ATHR690
AGLU691
AHOH2066
AHOH2067
BASP522
AGLY383
ALYS384
APRO439
AGLY440
APRO441
AGLN610
APHE645
ALYS685

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE XMP B 1694
ChainResidue
AASP522
BARG337
BGLY383
BLYS384
BPRO439
BGLY440
BPRO441
BARG524
BGLN610
BPHE645
BLYS685
BTHR689
BTHR690
BGLU691
BHOH2029
BHOH2057

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1695
ChainResidue
AARG276
AGLU279
AARG435
AHIS436
AHIS596
AARG600

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1696
ChainResidue
ATHR581
AGLY583
AVAL584

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1695
ChainResidue
BTHR581
BGLY583
BVAL584

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1696
ChainResidue
BARG276
BARG435
BHIS436
BHIS596
BARG600

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1697
ChainResidue
ASER244
AGLY246
AVAL247
AASP248
ASER249

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1697
ChainResidue
BSER244
BGLY246
BASP248
BSER249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: For GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605, ECO:0000269|PubMed:23816837
ChainResidueDetails
AGLU192
BCYS104
BHIS190
BGLU192
ACYS104
AHIS190

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00886
ChainResidueDetails
ASER244
BSER244

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:23816837
ChainResidueDetails
AARG337
AASP522
AGLN610
ALYS685
AGLU691
BARG337
BASP522
BGLN610
BLYS685
BGLU691

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ATHR318
BTHR318

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER332
BSER332

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PDB entries from 2024-06-12

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