3BLE

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 1003

Chain	Residue
A	HIS207
A	HIS209
A	HOH1047

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MLI A 701

Chain	Residue
A	HOH1083
A	HOH1099
A	HOH1102
A	ARG16
A	PRO177
A	THR179
A	HIS207
A	HIS209
A	HOH1047

---

Functional Information from PROSITE/UniProt

site_id	PS00815
Number of Residues	17
Details	AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGeQtrgvSfstseK

Chain	Residue	Details
A	LEU15-LYS31

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	261
Details	Domain: {"description":"Pyruvate carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18498255","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18498255","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18498255","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18498255","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19351325","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---