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1VKZ

Crystal structure of Phosphoribosylamine--glycine ligase (TM1250) from Thermotoga maritima at 2.30 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004637molecular_functionphosphoribosylamine-glycine ligase activity
A0005524molecular_functionATP binding
A0006189biological_process'de novo' IMP biosynthetic process
A0009113biological_processpurine nucleobase biosynthetic process
A0046872molecular_functionmetal ion binding
B0004637molecular_functionphosphoribosylamine-glycine ligase activity
B0005524molecular_functionATP binding
B0006189biological_process'de novo' IMP biosynthetic process
B0009113biological_processpurine nucleobase biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 401
ChainResidue
BLEU180

Functional Information from PROSITE/UniProt
site_idPS00184
Number of Residues8
DetailsGARS Phosphoribosylglycinamide synthetase signature. RLGDPEtE
ChainResidueDetails
AARG277-GLU284

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues126
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00138","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

254227

PDB entries from 2026-05-27

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