Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ILE

ISOLEUCYL-TRNA SYNTHETASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0002161molecular_functionaminoacyl-tRNA editing activity
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004822molecular_functionisoleucine-tRNA ligase activity
A0005524molecular_functionATP binding
A0006418biological_processtRNA aminoacylation for protein translation
A0006428biological_processisoleucyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1101
ChainResidue
ACYS181
ACYS184
ACYS389
ACYS392
AHOH1327

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1102
ChainResidue
AHOH1179
ACYS461
ACYS464
ACYS502
ACYS504

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PtaNGlPHVGHA
ChainResidueDetails
APRO47-ALA58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000305|PubMed:11584022, ECO:0007744|PDB:1JZQ
ChainResidueDetails
APRO46
AHIS57
AGLU550
AGLY551
AASP553
AGLN554
AHIS581

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, ECO:0007744|PDB:1JZS
ChainResidueDetails
ACYS181
ACYS184
ACYS389
ACYS392
ACYS502
ACYS504

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14672940
ChainResidueDetails
AHIS319
AASP328

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ
ChainResidueDetails
ACYS461

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1ILE
ChainResidueDetails
ACYS464

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS594

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 309
ChainResidueDetails
APRO46steric role, van der waals interaction
AASP85attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, steric role
ATRP518steric role, van der waals interaction
AGLN554hydrogen bond acceptor, steric role
ATRP558steric role, van der waals interaction
ALYS591attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
ALYS594attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon