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3UGJ

Formyl Glycinamide ribonucletide amidotransferase from Salmonella Typhimurum: 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
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 2001
ChainResidue
ALYS292
AGLU294
AASP318
ALYS776
AHOH1822
AHOH1867

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AASN297
AHIS298
ASER778
AHOH1395
AHOH1529
AHOH1624
AHIS216
ATHR295
AHIS296

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
ALYS327
AARG479
AASN1051
AHIS1053
AVAL1054
AHOH1590
AHOH1633
AHOH1660

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2004
ChainResidue
ATRP305
AARG1159
AARG1164
AHOH1350
AHOH1374
AHOH1939
AHOH1994

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 2009
ChainResidue
AHIS216
AGLY504
AALA505
ALYS776
AHOH1799
AHOH1867

site_idAC6
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP A 2005
ChainResidue
AVAL333
ATHR386
AGLY387
ATYR388
APHE389
ALYS649
ALEU652
AGLN668
APRO676
AALA678
AASP679
AGLU718
AASN722
ASER886
AHOH1297
AHOH1300
AHOH1345
AHOH1388
AHOH1400
AHOH1406
AHOH1451
AHOH1663
AMG2006
AMG2007
AMG2008
AHOH2093

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 2006
ChainResidue
AASP679
AASN722
AASP884
AADP2005

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 2007
ChainResidue
AGLU718
AHOH1297
AHOH1300
AADP2005

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 2008
ChainResidue
AHOH1394
AADP2005

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues253
DetailsDomain: {"description":"Glutamine amidotransferase type-1","evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15301531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22683785","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24223728","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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