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3A04

Crystal structure of tryptophanyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004830molecular_functiontryptophan-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006436biological_processtryptophanyl-tRNA aminoacylation
A0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 A 373
ChainResidue
AGLY285
AGLY286
ACYS303
ACYS327
AILE332
ACYS334
ACYS337

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 374
ChainResidue
AGLU343
AGLU346
AGLU69
AHIS209

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 375
ChainResidue
AGLU13
AHIS307
AHOH584
AHOH653

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"'HIGH' region"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsMotif: {"description":"'KMSKS' region"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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