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1KOG

Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator

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
E0000166molecular_functionnucleotide binding
E0004812molecular_functionaminoacyl-tRNA ligase activity
E0004829molecular_functionthreonine-tRNA ligase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0006418biological_processtRNA aminoacylation for protein translation
E0006435biological_processthreonyl-tRNA aminoacylation
F0000166molecular_functionnucleotide binding
F0004812molecular_functionaminoacyl-tRNA ligase activity
F0004829molecular_functionthreonine-tRNA ligase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0006418biological_processtRNA aminoacylation for protein translation
F0006435biological_processthreonyl-tRNA aminoacylation
G0000166molecular_functionnucleotide binding
G0004812molecular_functionaminoacyl-tRNA ligase activity
G0004829molecular_functionthreonine-tRNA ligase activity
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0006418biological_processtRNA aminoacylation for protein translation
G0006435biological_processthreonyl-tRNA aminoacylation
H0000166molecular_functionnucleotide binding
H0004812molecular_functionaminoacyl-tRNA ligase activity
H0004829molecular_functionthreonine-tRNA ligase activity
H0005524molecular_functionATP binding
H0005737cellular_componentcytoplasm
H0006418biological_processtRNA aminoacylation for protein translation
H0006435biological_processthreonyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
ACYS334
AHIS385
ATYR462
AHIS511
ATSB2002

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1
ChainResidue
BCYS334
BHIS385
BHIS511
BTSB3002

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 1
ChainResidue
CCYS334
CHIS385
CTYR462
CHIS511
CTSB4002

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1
ChainResidue
DCYS334
DHIS385
DHIS511
DTSB5002

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 1
ChainResidue
ECYS334
EHIS385
EHIS511
ETSB6002

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN F 1
ChainResidue
FCYS334
FHIS385
FTYR462
FHIS511
FTSB7002

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN G 1
ChainResidue
GCYS334
GHIS385
GTYR462
GHIS511
GTSB8002

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN H 1
ChainResidue
HCYS334
HHIS385
HTYR462
HHIS511
HTSB9002

site_idAC9
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TSB A 2002
ChainResidue
AZN1
AMET332
ACYS334
AARG363
AGLU365
AMET374
AVAL376
APHE379
AGLN381
AASP383
AALA384
AHIS385
ATYR462
AGLN479
ACYS480
ATHR482
AGLN484
AHIS511
AARG512
AGLY516
ASER517
AARG520

site_idBC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TSB B 3002
ChainResidue
BZN1
BMET332
BCYS334
BARG363
BGLU365
BMET374
BVAL376
BPHE379
BGLN381
BASP383
BALA384
BHIS385
BTYR462
BGLN479
BCYS480
BTHR482
BGLN484
BHIS511
BARG512
BGLY516
BSER517
BARG520

site_idBC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE TSB C 4002
ChainResidue
CGLY516
CSER517
CARG520
CZN1
CMET332
CCYS334
CARG363
CGLU365
CMET374
CVAL376
CPHE379
CGLN381
CASP383
CALA384
CHIS385
CTYR462
CGLN479
CCYS480
CGLN484
CHIS511
CARG512

site_idBC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TSB D 5002
ChainResidue
DZN1
DMET332
DCYS334
DARG363
DGLU365
DMET374
DVAL376
DPHE379
DGLN381
DASP383
DALA384
DHIS385
DTYR462
DGLN479
DCYS480
DTHR482
DGLN484
DHIS511
DARG512
DGLY516
DSER517
DARG520

site_idBC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE TSB E 6002
ChainResidue
EZN1
EMET332
ECYS334
EARG363
EGLU365
EMET374
EVAL376
EPHE379
EGLN381
EASP383
EALA384
EHIS385
ETYR462
EGLN479
ECYS480
ETHR482
EGLN484
EHIS511
EARG512
EALA513
EGLY516
ESER517
EARG520

site_idBC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TSB F 7002
ChainResidue
FZN1
FMET332
FCYS334
FARG363
FGLU365
FMET374
FVAL376
FPHE379
FGLN381
FASP383
FALA384
FHIS385
FTYR462
FGLN479
FCYS480
FTHR482
FGLN484
FHIS511
FARG512
FGLY516
FSER517
FARG520

site_idBC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TSB G 8002
ChainResidue
GZN1
GMET332
GCYS334
GARG363
GGLU365
GMET374
GVAL376
GPHE379
GGLN381
GASP383
GALA384
GHIS385
GTYR462
GGLN479
GCYS480
GTHR482
GGLN484
GHIS511
GARG512
GGLY516
GSER517
GARG520

site_idBC7
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TSB H 9002
ChainResidue
HZN1
HMET332
HCYS334
HARG363
HGLU365
HMET374
HVAL376
HPHE379
HGLN381
HASP383
HALA384
HHIS385
HTYR462
HGLN479
HCYS480
HTHR482
HGLN484
HHIS511
HARG512
HGLY516
HSER517
HARG520

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2328
DetailsRegion: {"description":"Catalytic","evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues856
DetailsRegion: {"description":"Anticodon recognition","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues288
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11953757","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QF6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues232
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10881191","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11136973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11953757","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10881191","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11136973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
AARG363

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
BARG363

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
CARG363

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
DARG363

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
EARG363

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
FARG363

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
GARG363

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
HARG363

site_idMCSA1
Number of Residues7
DetailsM-CSA 540
ChainResidueDetails

site_idMCSA2
Number of Residues7
DetailsM-CSA 540
ChainResidueDetails

site_idMCSA3
Number of Residues7
DetailsM-CSA 540
ChainResidueDetails

site_idMCSA4
Number of Residues7
DetailsM-CSA 540
ChainResidueDetails

site_idMCSA5
Number of Residues7
DetailsM-CSA 540
ChainResidueDetails

site_idMCSA6
Number of Residues7
DetailsM-CSA 540
ChainResidueDetails

site_idMCSA7
Number of Residues7
DetailsM-CSA 540
ChainResidueDetails

site_idMCSA8
Number of Residues7
DetailsM-CSA 540
ChainResidueDetails

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PDB entries from 2025-11-05

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