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6SPO

Structure of the Escherichia coli methionyl-tRNA synthetase complexed with methionine

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 Residues7
Detailsbinding site for residue CIT A 602
ChainResidue
AHOH951
AHOH970
AGLN63
ALYS132
ALYS465
AHOH746
AHOH798

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 603
ChainResidue
AGLN458
AARG469
AHOH734
AHOH812
AHOH892

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 604
ChainResidue
ATYR128
AGLY133
AALA235
AARG469
AHOH892
AHOH1065
AHOH1290

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 605
ChainResidue
AHIS98
ASER99
AGLU100
AARG103

site_idAC6
Number of Residues12
Detailsbinding site for residue MET A 606
ChainResidue
ALEU13
ATYR15
AASP52
ATRP253
AALA256
APRO257
ATYR260
AILE297
AHOH909
AHOH916
AHOH1113
AHOH1156

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

223166

PDB entries from 2024-07-31

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