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2F2A

Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Gln

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004359molecular_functionglutaminase activity
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0030956cellular_componentglutamyl-tRNA(Gln) amidotransferase complex
A0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
A0070681biological_processglutaminyl-tRNAGln biosynthesis via transamidation
B0003824molecular_functioncatalytic activity
B0006412biological_processtranslation
B0016874molecular_functionligase activity
B0016884molecular_functioncarbon-nitrogen ligase activity, with glutamine as amido-N-donor
B0030956cellular_componentglutamyl-tRNA(Gln) amidotransferase complex
B0050566molecular_functionasparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
B0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
B0070681biological_processglutaminyl-tRNAGln biosynthesis via transamidation
C0006412biological_processtranslation
C0006450biological_processregulation of translational fidelity
C0070681biological_processglutaminyl-tRNAGln biosynthesis via transamidation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BHIS12
BGLU124
BGLU150
BHOH636
BHOH637
BHOH638

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GLN A 501
ChainResidue
ASER154
AASP174
ATHR175
AGLY176
AGLY177
ASER178
APHE206
ATYR309
ATYR310
AARG358
AASP425
AHOH508
AHOH529
AHOH701
AALA128
AMET129
AGLY130

Functional Information from PROSITE/UniProt
site_idPS00571
Number of Residues32
DetailsAMIDASES Amidases signature. GGSSGGsAAaVAaglvplSlGsDtGgSIRqPA
ChainResidueDetails
AGLY152-ALA183

site_idPS01234
Number of Residues15
DetailsGATB Glutamyl-tRNA(Gln) amidotransferase subunit B signature. LNRqgtPLIEIvSeP
ChainResidueDetails
BLEU141-PRO155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_00120","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_00120","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00120","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16809541","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2F2A","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16809541","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DF4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16809541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19906721","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DF4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2DQN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2F2A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G5H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G5I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IP4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16809541","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2G5I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

259693

PDB entries from 2026-09-16

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