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3BLF

Crystal structure of the catalytic domain of LiCMS in complexed with pyruvate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0019752biological_processcarboxylic acid metabolic process
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1003
ChainResidue
AASP17
AHIS207
AHIS209
AHOH1005

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR A 1004
ChainResidue
AHIS207
AHIS209
AARG16
AASP17
ATYR144
APRO177
ATHR179

Functional Information from PROSITE/UniProt
site_idPS00815
Number of Residues17
DetailsAIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGeQtrgvSfstseK
ChainResidueDetails
ALEU15-LYS31

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues261
DetailsDomain: {"description":"Pyruvate carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01151","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18498255","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18498255","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18498255","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18498255","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19351325","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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