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4DS3

Crystal Structure of Phosphoribosylglycinamide formyltransferase from Brucella melitensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AARG22
APRO27
ALYS174
AHIS177
AARG178
AHOH560

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AARG61
ALYS67
AHOH491

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AARG98
APRO119
AGLY120
AARG126
AHOH507
AHOH537

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
AHIS122
AHIS124
AGLN125
AHOH504

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
AGLY12
AGLY13
AGLY14
ASER15
AASN16
AHOH406
AHOH423
AHOH428
AHOH509
AHOH543

Functional Information from PROSITE/UniProt
site_idPS00373
Number of Residues24
DetailsGART Phosphoribosylglycinamide formyltransferase active site. GcTVhLVtEgMDeGpiLaqaavpV
ChainResidueDetails
AGLY136-VAL159

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PDB entries from 2024-07-24

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