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5GL7

Crystal structure of a truncated human cytosolic methionyl-tRNA synthetase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004825molecular_functionmethionine-tRNA ligase activity
A0005524molecular_functionATP binding
A0006418biological_processtRNA aminoacylation for protein translation
A0006431biological_processmethionyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 901
ChainResidue
ACYS389
ACYS392
ACYS435
ACYS438

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 902
ChainResidue
ACYS405
ACYS408
ACYS418
ACYS421

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 903
ChainResidue
AGLN302
ASER779
AARG299

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 904
ChainResidue
AGLU263
AGLN381
AASP382
ATHR383
AHOH1122
AHOH1176

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PyvNNvPHLGNI
ChainResidueDetails
APRO273-ILE284

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS596

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q68FL6
ChainResidueDetails
ASER825

226707

PDB entries from 2024-10-30

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