Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3H99

Structure of a mutant methionyl-tRNA synthetase with modified specificity 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 Residues13
DetailsBINDING SITE FOR RESIDUE MET A 602
ChainResidue
ASER13
AHOH1469
AHOH1489
AHOH1506
AHOH1938
ATYR15
AASP52
ATRP253
AALA256
APRO257
AILE297
AHOH1442
AHOH1462

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
ACYS145
ACYS148
ACYS158
AVAL160
ACYS161

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT A 603
ChainResidue
APRO137
AASP138
AARG233
AHOH1436
AHOH1463
AHOH1480
AHOH1495
AHOH1520
AHOH1536
AHOH1589
AHOH1929
AHOH1932
AHOH1940

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT A 604
ChainResidue
AGLN63
ALYS132
AHOH1568
AHOH1586
AHOH1596
AHOH1606
AHOH1662
AHOH1663
AHOH1978
AHOH2012

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 Residues10
DetailsMotif: {"description":"'HIGH' region","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"7932711","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11243794","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12946347","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F4L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PG2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10600385","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11243794","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12946347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8515465","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8515466","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F4L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MEA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PFU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QQT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"2254937","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a8h
ChainResidueDetails
ALYS335
ALYS332

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a8h
ChainResidueDetails
ALYS335

250359

PDB entries from 2026-03-11

PDB statisticsPDBj update infoContact PDBjnumon