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6SPP

Structure of the Escherichia coli methionyl-tRNA synthetase variant VI298

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 601
ChainResidue
ACYS145
ACYS148
ACYS158
ACYS161

site_idAC2
Number of Residues10
Detailsbinding site for residue CIT A 602
ChainResidue
AHOH908
AHOH1008
AHOH1021
AHOH1041
AHOH1129
ATHR56
APRO137
AARG139
AARG233
ATYR251

site_idAC3
Number of Residues6
Detailsbinding site for residue CIT A 603
ChainResidue
AGLN63
ALYS132
AHOH815
AHOH823
AHOH839
AHOH862

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 604
ChainResidue
ALEU13
AALA256
ATYR260
AHIS301

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PyaNGsIHLGHM
ChainResidueDetails
APRO14-MET25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ACYS145
ACYS148
ACYS158
ACYS161
ALYS335

221371

PDB entries from 2024-06-19

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