5MY2

KS-MAT DI-DOMAIN OF MOUSE FAS

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	13
Details	binding site for residue COA D 900

Chain	Residue
D	MET499
D	LEU766
D	LEU767
D	LYS772
D	ARG773
D	HIS580
D	MET620
D	ALA622
D	ASN644
D	ASP647
D	THR648
D	THR650
D	PHE671

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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. GPSiaLDtACSSSllAL

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
A	CYS161
D	CYS161
D	HIS293
D	HIS331
A	HIS293
A	HIS331
B	CYS161
B	HIS293
B	HIS331
C	CYS161
C	HIS293
C	HIS331

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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	12
Details	BINDING: BINDING => ECO:0000269|PubMed:31811668, ECO:0007744|PDB:6ROP

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

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site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337

Chain	Residue	Details
A	LYS59
A	LYS790
B	LYS59
B	LYS790
C	LYS59
C	LYS790
D	LYS59
D	LYS790

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site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49327

Chain	Residue	Details
A	SER63
A	SER207
B	SER63
B	SER207
C	SER63
C	SER207
D	SER63
D	SER207

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site_id	SWS_FT_FI6
Number of Residues	16
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P49327

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

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site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	SER725
B	SER725
C	SER725
D	SER725

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