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4N0H

Crystal structure of S. cerevisiae mitochondrial GatFAB

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0006412biological_processtranslation
A0007029biological_processendoplasmic reticulum organization
A0016874molecular_functionligase activity
A0030956cellular_componentglutamyl-tRNA(Gln) amidotransferase complex
A0032543biological_processmitochondrial translation
A0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
A0070681biological_processglutaminyl-tRNAGln biosynthesis via transamidation
B0003824molecular_functioncatalytic activity
B0016874molecular_functionligase activity
B0016884molecular_functioncarbon-nitrogen ligase activity, with glutamine as amido-N-donor
F0005739cellular_componentmitochondrion
F0030956cellular_componentglutamyl-tRNA(Gln) amidotransferase complex
F0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
F0070681biological_processglutaminyl-tRNAGln biosynthesis via transamidation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NO3 A 501
ChainResidue
AARG233
AHOH641
FLEU46
APHE243
ASER244
AMET248
APHE252
AHIS253
ATYR256
APRO391
AHOH632

Functional Information from PROSITE/UniProt
site_idPS00571
Number of Residues32
DetailsAMIDASES Amidases signature. GGSSSGaAAsVAcdlvdfAlGtDtGgSVRlPA
ChainResidueDetails
AGLY128-ALA159

site_idPS01234
Number of Residues15
DetailsGATB Glutamyl-tRNA(Gln) amidotransferase subunit B signature. LNRsnvPLIELvTkP
ChainResidueDetails
BLEU177-PRO191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_03150
ChainResidueDetails
ALYS52
ASER130

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|HAMAP-Rule:MF_03150
ChainResidueDetails
ASER154

221716

PDB entries from 2024-06-26

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