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	12
Details	ACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348

Chain	Residue	Details
B	HIS293
B	HIS331
C	CYS161
C	HIS293
C	HIS331
D	CYS161
D	HIS293
D	HIS331
A	CYS161
A	HIS293
A	HIS331
B	CYS161

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: For malonyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU10022

Chain	Residue	Details
A	SER581
B	SER581
C	SER581
D	SER581

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site_id	SWS_FT_FI3
Number of Residues	4
Details	ACT_SITE: Proton acceptor; for dehydratase activity => ECO:0000255|PROSITE-ProRule:PRU01363

Chain	Residue	Details
A	HIS878
B	HIS878
C	HIS878
D	HIS878

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P19096

Chain	Residue	Details
C	ARG773
D	ASP647
D	PHE671
D	ARG773
A	ASP647
A	PHE671
A	ARG773
B	ASP647
B	PHE671
B	ARG773
C	ASP647
C	PHE671

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER63
B	SER63
C	SER63
D	SER63

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS70
A	LYS298
A	LYS436
A	LYS528
A	LYS673
B	LYS70
B	LYS298
B	LYS436
B	LYS528
B	LYS673
C	LYS70
C	LYS298
C	LYS436
C	LYS528
C	LYS673
D	LYS70
D	LYS298
D	LYS436
D	LYS528
D	LYS673

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER207
B	SER207
C	SER207
D	SER207

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19096

Chain	Residue	Details
A	SER725
B	SER725
C	SER725
D	SER725

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