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3UJN

Formyl Glycinamide Ribonucleotide Amidotransferase from Salmonella Typhimurium : Role of the ATP complexation and glutaminase domain in catalytic coupling

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004642molecular_functionphosphoribosylformylglycinamidine synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0006541biological_processglutamine metabolic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
ATHR295
AASN297
AHIS298
ALYS409
ASER778
AHOH1437
AHOH1499
AHOH1511

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP A 2005
ChainResidue
ATHR386
AGLY387
ATYR388
ALYS649
ALEU652
AVAL653
AGLN668
APRO676
AALA678
AASP679
AGLU718
AASN722
ASER886
AHOH1533
AMG2006
AMG2007
AMG2008
AVAL333

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 2006
ChainResidue
AGLU718
AADP2005

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 2007
ChainResidue
ASER886
AADP2005

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2008
ChainResidue
AASP679
AASN722
AASP884
ASER886
AADP2005

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2009
ChainResidue
ASER12
AALA13
APHE14
AASN998
AHIS1161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00419
ChainResidueDetails
ACYG1135

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00419
ChainResidueDetails
AHIS1260
AGLU1262

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00419
ChainResidueDetails
AGLY307

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ATHR386
AALA678
ASER886

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728
ChainResidueDetails
AASP679
AGLU718
AASN722
AASP884

217705

PDB entries from 2024-03-27

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