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6LBP

Structure of the Glutamine Phosphoribosylpyrophosphate Amidotransferase from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0004044molecular_functionamidophosphoribosyltransferase activity
A0009113biological_processpurine nucleobase biosynthetic process
B0004044molecular_functionamidophosphoribosyltransferase activity
B0009113biological_processpurine nucleobase biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SF4 A 600
ChainResidue
ACYS323
ACYS469
ATYR471
ACYS520
AALA522
ACYS523

site_idAC2
Number of Residues6
Detailsbinding site for residue SF4 B 600
ChainResidue
BCYS520
BALA522
BCYS523
BCYS323
BCYS469
BTYR471

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VVVVDDSIVRGtT
ChainResidueDetails
AVAL428-THR440

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues440
DetailsDomain: {"description":"Glutamine amidotransferase type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00609","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU00609","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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