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2YW2

Crystal structure of GAR synthetase from Aquifex aeolicus in complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004637molecular_functionphosphoribosylamine-glycine ligase activity
A0005524molecular_functionATP binding
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0009113biological_processpurine nucleobase biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004637molecular_functionphosphoribosylamine-glycine ligase activity
B0005524molecular_functionATP binding
B0006164biological_processpurine nucleotide biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0009113biological_processpurine nucleobase biosynthetic process
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 645
ChainResidue
AARG11
AGLU71
AARG287
AASP290
AARG378
AHOH666
AHOH754

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 646
ChainResidue
BARG287
BASP290
BARG378
BHOH670
BHOH746
BHOH760
BHOH809
BHOH811
BARG11
BGLU71

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP A 646
ChainResidue
ALYS103
AVAL141
ALYS143
AALA148
AGLY150
ALYS151
AGLY152
AALA153
AGLU185
AGLU186
APHE187
ALEU188
AGLU192
ALYS214
AASN224
AGLU283
AHOH676
AHOH702
AHOH720

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP B 647
ChainResidue
BLYS103
BLYS143
BGLY150
BLYS151
BGLY152
BALA153
BGLU185
BGLU186
BPHE187
BLEU188
BGLU192
BLYS214
BASN224
BHOH679
BHOH699
BHOH700
BHOH743
BHOH773
BHOH777
BHOH792

Functional Information from PROSITE/UniProt
site_idPS00184
Number of Residues8
DetailsGARS Phosphoribosylglycinamide synthetase signature. RLGDPEaQ
ChainResidueDetails
AARG287-GLN294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00138
ChainResidueDetails
AVAL133
AGLU283
AASN285
BVAL133
BGLU283
BASN285

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PDB entries from 2025-06-18

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