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5K0S

Crystal structure of methionyl-tRNA synthetase MetRS from Brucella melitensis in complex with inhibitor Chem 1312

Replaces:  4LNE
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004825molecular_functionmethionine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006431biological_processmethionyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004825molecular_functionmethionine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006431biological_processmethionyl-tRNA aminoacylation
C0000166molecular_functionnucleotide binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004825molecular_functionmethionine-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006412biological_processtranslation
C0006418biological_processtRNA aminoacylation for protein translation
C0006431biological_processmethionyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue 0OU A 601
ChainResidue
AILE12
AALA233
ATYR237
AHIS269
ATYR14
AASP51
AHIS53
AGLY54
AMET227
ATYR228
AVAL229
AASP232

site_idAC2
Number of Residues16
Detailsbinding site for residue 0OU B 601
ChainResidue
BALA11
BILE12
BTYR14
BASP51
BHIS53
BGLY54
BMET227
BTYR228
BVAL229
BASP232
BALA233
BTYR237
BHIS269
BHOH726
BHOH727
BHOH757

site_idAC3
Number of Residues12
Detailsbinding site for residue 0OU C 601
ChainResidue
CILE12
CTYR14
CASP51
CHIS53
CGLY54
CMET227
CTYR228
CVAL229
CASP232
CALA233
CTYR237
CHIS269

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..NGkPHIGHA
ChainResidueDetails
APRO15-ALA24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01228
ChainResidueDetails
ALYS303
BLYS303
CLYS303

219140

PDB entries from 2024-05-01

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