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6HXK

Structure of the citryl-CoA lyase core module of human ATP citrate lyase in complex with citrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
C0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
D0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue FLC A 1200
ChainResidue
AHIS900
AHOH1373
AHOH1396
AHOH1407
AHOH1408
CARG1085
AVAL904
APHE935
AGLY936
AASP1026
APHE1061
AARG1065
AHOH1304
AHOH1354

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 1201
ChainResidue
ALYS964
ALYS968
AEDO1202

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 1202
ChainResidue
ALEU969
AILE970
AILE973
AEDO1201

site_idAC4
Number of Residues12
Detailsbinding site for residue FLC B 1201
ChainResidue
BHIS900
BVAL904
BPHE935
BGLY936
BPHE1061
BARG1065
BHOH1306
BHOH1326
BHOH1379
BHOH1382
BHOH1384
DARG1085

site_idAC5
Number of Residues5
Detailsbinding site for residue PGE B 1202
ChainResidue
AGLU866
BGLN888
BGLU891
BMET892
BHOH1322

site_idAC6
Number of Residues12
Detailsbinding site for residue 1PE C 1201
ChainResidue
AASN982
BGLN850
CGLN888
CGLU891
CMET892
CTYR993
CHOH1398
DPHE863
DGLU866
DGLY868
DHOH1368
DHOH1410

site_idAC7
Number of Residues11
Detailsbinding site for residue FLC C 1202
ChainResidue
AARG1085
CHIS900
CVAL904
CPHE935
CGLY936
CPHE1061
CARG1065
CHOH1304
CHOH1334
CHOH1352
CHOH1392

site_idAC8
Number of Residues3
Detailsbinding site for residue PEG C 1203
ChainResidue
AHIS975
CGLN996
CHIS997

site_idAC9
Number of Residues11
Detailsbinding site for residue FLC D 1200
ChainResidue
BARG1085
DHIS900
DVAL904
DPHE935
DGLY936
DASP1026
DARG1065
DHOH1320
DHOH1335
DHOH1354
DHOH1400

site_idAD1
Number of Residues8
Detailsbinding site for residue PGE D 1201
ChainResidue
CGLU866
CHOH1355
CHOH1395
DGLN888
DGLU891
DMET892
DTYR993
DHOH1406

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO D 1202
ChainResidue
DALA855
DMET857
DLEU875
DGLN879
DHOH1392

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER839
BSER839
CSER839
DSER839

site_idSWS_FT_FI2
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS948
DLYS948
DLYS968
DLYS1077
ALYS968
ALYS1077
BLYS948
BLYS968
BLYS1077
CLYS948
CLYS968
CLYS1077

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91V92
ChainResidueDetails
ALYS978
BLYS978
CLYS978
DLYS978

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER1100
BSER1100
CSER1100
DSER1100

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PDB entries from 2024-07-10

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