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3MWE

Truncated Human ATP-Citrate Lyase with Tartrate Bound

Functional Information from GO Data
ChainGOidnamespacecontents
B0003824molecular_functioncatalytic activity
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 426
ChainResidue
AASP257
ASER260
AALA262
AHOH624

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TLA A 427
ChainResidue
ATHR348
AARG379
AHOH531
AHOH1362
AGLY309
AALA310
AALA345
AASN346
APHE347

Functional Information from PROSITE/UniProt
site_idPS00399
Number of Residues17
DetailsSUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GtcAtmfssevQFGHAG
ChainResidueDetails
BGLY746-GLY762

site_idPS01216
Number of Residues30
DetailsSUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGGMSnElnniisrttdGvyegVAIGGD
ChainResidueDetails
BSER661-ASP690

site_idPS01217
Number of Residues25
DetailsSUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GrIwtMvAGGGASvvysDtIcdl.GG
ChainResidueDetails
AGLY273-GLY297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues261
DetailsDomain: {"description":"ATP-grasp"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22102020","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20558738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22102020","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20558738","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q91V92","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"27664236","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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