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4HWT

Crystal structure of human Threonyl-tRNA synthetase bound to a novel inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004829molecular_functionthreonine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006418biological_processtRNA aminoacylation for protein translation
A0006435biological_processthreonyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004829molecular_functionthreonine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006418biological_processtRNA aminoacylation for protein translation
B0006435biological_processthreonyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 801
ChainResidue
ACYS446
AHIS497
AHIS623
A1B2802

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 1B2 A 802
ChainResidue
AHIS497
ATYR573
AASP578
AILE579
AGLN590
ACYS591
AALA592
AGLN595
AHIS623
AZN801
AHOH918
AMET444
ACYS446
AARG475
AGLN493
AASP495

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 801
ChainResidue
BCYS446
BHIS497
BHIS623
B1B2802

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 1B2 B 802
ChainResidue
BMET444
BCYS446
BARG475
BGLN493
BASP495
BHIS497
BTYR573
BLYS576
BASP578
BILE579
BGLN590
BCYS591
BALA592
BTHR593
BGLN595
BHIS623
BZN801

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR486
BTHR486

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER735
BSER735

222415

PDB entries from 2024-07-10

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