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1NYQ

Structure of Staphylococcus aureus threonyl-tRNA synthetase complexed with an analogue of threonyl adenylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004829molecular_functionthreonine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006435biological_processthreonyl-tRNA aminoacylation
A0016740molecular_functiontransferase activity
A0043039biological_processtRNA aminoacylation
A0046872molecular_functionmetal ion binding
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004829molecular_functionthreonine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006435biological_processthreonyl-tRNA aminoacylation
B0016740molecular_functiontransferase activity
B0043039biological_processtRNA aminoacylation
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
ACYS336
AHIS387
AHIS517
ATSB1002

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2001
ChainResidue
BCYS336
BHIS387
BHIS517
BTSB2002

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE TSB A 1002
ChainResidue
ACYS336
AARG365
AARG377
AVAL378
AMET381
ALEU383
AASP385
AHIS387
ATYR468
ATHR485
ALEU486
AGLN490
AHIS517
ASER522
ATHR523
AARG526
AZN1001
AHOH1040
AMET334

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TSB B 2002
ChainResidue
BMET334
BCYS336
BARG365
BGLU367
BGLN376
BARG377
BVAL378
BMET381
BLEU383
BASP385
BHIS387
BTYR468
BTHR485
BLEU486
BTHR488
BGLN490
BHIS517
BSER522
BTHR523
BARG526
BZN2001
BHOH2013

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:12875846
ChainResidueDetails
ACYS336
AHIS387
AHIS517
BCYS336
BHIS387
BHIS517

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12875846
ChainResidueDetails
AARG365
BLYS471
BTHR485
BSER522
AARG377
ATYR468
ALYS471
ATHR485
ASER522
BARG365
BARG377
BTYR468

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
AARG365

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
BARG365

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PDB entries from 2024-07-17

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