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4TTV

Crystal structure of human ThrRS complexing with a bioengineered macrolide BC194

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
C0000166molecular_functionnucleotide binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004829molecular_functionthreonine-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006418biological_processtRNA aminoacylation for protein translation
C0006435biological_processthreonyl-tRNA aminoacylation
D0000166molecular_functionnucleotide binding
D0004812molecular_functionaminoacyl-tRNA ligase activity
D0004829molecular_functionthreonine-tRNA ligase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006418biological_processtRNA aminoacylation for protein translation
D0006435biological_processthreonyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue BC9 A 801
ChainResidue
ASER386
ALEU567
AHIS590
AGLY387
AHIS388
ACYS413
AARG442
AGLN460
ATYR540
ATHR560
AASP564

site_idAC2
Number of Residues3
Detailsbinding site for residue ZN A 802
ChainResidue
ACYS413
AHIS464
AHIS590

site_idAC3
Number of Residues10
Detailsbinding site for residue BC9 B 801
ChainResidue
BGLY387
BHIS388
BCYS413
BARG442
BGLN460
BTYR540
BTHR560
BASP564
BLEU567
BHIS590

site_idAC4
Number of Residues3
Detailsbinding site for residue ZN B 802
ChainResidue
BCYS413
BHIS464
BHIS590

site_idAC5
Number of Residues9
Detailsbinding site for residue BC9 C 801
ChainResidue
CHIS388
CMET411
CCYS413
CARG442
CTYR540
CTHR560
CASP564
CLEU567
CHIS590

site_idAC6
Number of Residues3
Detailsbinding site for residue ZN C 802
ChainResidue
CCYS413
CHIS464
CHIS590

site_idAC7
Number of Residues9
Detailsbinding site for residue BC9 D 801
ChainResidue
DHIS388
DMET411
DCYS413
DARG442
DTYR540
DTHR560
DASP564
DLEU567
DHIS590

site_idAC8
Number of Residues3
Detailsbinding site for residue ZN D 802
ChainResidue
DCYS413
DHIS464
DHIS590

site_idAC9
Number of Residues7
Detailsbinding site for Ligand ASN B 533 bound to ASN B 497
ChainResidue
BASN497
BLEU498
BSER499
BLEU532
BSER534
BGLY535
BASP536

site_idAD1
Number of Residues13
Detailsbinding site for Di-peptide GLN C 666 and ASN C 693
ChainResidue
CILE662
CARG663
CASN664
CALA665
CLEU667
CALA668
CGLN669
CARG689
CTHR690
CARG691
CASP692
CLYS694
CVAL695

site_idAD2
Number of Residues12
Detailsbinding site for Di-peptide GLN D 666 and ASN D 693
ChainResidue
DILE662
DARG663
DASN664
DALA665
DLEU667
DALA668
DGLN669
DARG689
DTHR690
DARG691
DASP692
DLYS694

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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