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6HXM

Structure of the citryl-CoA lyase core module of human ATP citrate lyase in complex with citrate and CoASH in space group C2221

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
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue COA B 1200
ChainResidue
BALA938
BLYS1017
BLYS1018
BASN1020
BLEU1021
BASN1024
BASP1026
BHOH1328
BHOH1377
BHOH1396
BHOH1418
BLYS964
BHOH1442
BHOH1460
BHOH1469
BHOH1514
BLYS965
BLEU969
BILE970
BMET971
BGLY972
BILE973
BGLY974

site_idAC2
Number of Residues13
Detailsbinding site for residue FLC B 1201
ChainResidue
BHIS900
BVAL904
BPHE935
BGLY936
BASP1026
BPHE1061
BARG1065
BARG1085
BHOH1301
BHOH1355
BHOH1402
BHOH1410
BHOH1469

site_idAC3
Number of Residues37
Detailsbinding site for residues COA A 1200 and FLC A 1201
ChainResidue
AHIS900
AVAL904
AASP933
AARG934
APHE935
AGLY936
AALA938
ALYS964
ALEU969
AILE970
AGLY972
AILE973
AGLY974
AHIS975
AARG976
AARG986
AASN1020
ALEU1021
AASN1024
AVAL1025
AASP1026
AARG1065
AARG1085
AHOH1303
AHOH1305
AHOH1307
AHOH1311
AHOH1337
AHOH1349
AHOH1352
AHOH1356
AHOH1358
AHOH1385
AHOH1399
AHOH1403
AHOH1417
AHOH1460

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER839
BSER839

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS948
ALYS968
ALYS1077
BLYS948
BLYS968
BLYS1077

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91V92
ChainResidueDetails
ALYS978
BLYS978

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER1100
BSER1100

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PDB entries from 2024-07-31

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