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2GI3

Crystal structure of Glutamyl-tRNA(Gln) amidotransferase subunit A (tm1272) from THERMOTOGA MARITIMA at 1.80 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0006412biological_processtranslation
A0016874molecular_functionligase activity
A0030956cellular_componentglutamyl-tRNA(Gln) amidotransferase complex
A0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 476
ChainResidue
AGLY419
AARG443

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 478
ChainResidue
ALYS57
AILE212
AMPD481
AHOH780

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MPD A 479
ChainResidue
ATYR381
AASP382
AARG442
ALYS448
AHOH627
AHOH761
AARG230
ASER379
AGLN380

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 480
ChainResidue
AARG122
ATHR350
ALYS400
AHOH742

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 481
ChainResidue
ALYS57
APHE58
AGLU215
ALEU235
AACT478
AHOH779

Functional Information from PROSITE/UniProt
site_idPS00571
Number of Residues32
DetailsAMIDASES Amidases signature. GGSSGGsAAaVSagmvvaAlGsDtGgSVRqPA
ChainResidueDetails
AGLY139-ALA170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
ALYS66
ASER141

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000250
ChainResidueDetails
ASER165

219869

PDB entries from 2024-05-15

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