2QHV

Structural Basis of Octanoic Acid Recognition by Lipoate-Protein Ligase B

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0009249	biological_process	protein lipoylation
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0033819	molecular_function	lipoyl(octanoyl) transferase activity
A	0036211	biological_process	protein modification process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OC9 A 1001

Chain	Residue
A	ARG75
A	GLY77
A	ASP78
A	ALA139
A	GLY141
A	GLY152
A	PHE153
A	HOH1124
A	HOH1147

---

Functional Information from PROSITE/UniProt

site_id	PS01313
Number of Residues	16
Details	LIPB Lipoate-protein ligase B signature. RGGdvTYHgpGQlVgY

Chain	Residue	Details
A	ARG75-TYR90

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	179
Details	Domain: {"description":"BPL/LPL catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01067","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_00013","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	11
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Lowers pKa of active site Cys","evidences":[{"source":"HAMAP-Rule","id":"MF_00013","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---