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2XD4

Nucleotide-bound Structures of Bacillus subtilis Glycinamide Ribonucleotide Synthetase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ADP A 461
ChainResidue
ALYS103
ALYS214
AMET273
AILE282
AGLU283
AMG451
AMG453
AHOH2070
AHOH2071
AVAL141
ALYS143
AGLY150
AVAL153
AGLU185
AGLU186
ALEU188
AGLU192

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 451
ChainResidue
AGLU283
AASN285
AADP461
AHOH2070

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 452
ChainResidue
AHIS167
AASP172
AHOH2038

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 453
ChainResidue
ALYS214
AGLU283
AADP461

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues206
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_00138","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues63
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00138","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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