3HHD

Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
A	0006633	biological_process	fatty acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
B	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
B	0006633	biological_process	fatty acid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
C	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
C	0006633	biological_process	fatty acid biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
D	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
D	0006633	biological_process	fatty acid biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 964

Chain	Residue
C	TYR589

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL D 964

Chain	Residue
D	HOH1539

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Functional Information from PROSITE/UniProt

site_id	PS00606
Number of Residues	17
Details	KS3_1 Ketosynthase family 3 (KS3) active site signature. GPSiaLDtACSSSlmAL

Chain	Residue	Details
A	GLY152-LEU168

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1552
Details	Region: {"description":"Acyl and malonyl transferases","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"For malonyltransferase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU10022","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P19096","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19096","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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