2JFK

Structure of the MAT domain of human FAS with malonyl-CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016740	molecular_function	transferase activity
B	0016740	molecular_function	transferase activity
C	0016740	molecular_function	transferase activity
D	0016740	molecular_function	transferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE COA A1820

Chain	Residue
A	GLY500
A	ARG676

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE COA B1823

Chain	Residue
B	LYS673
B	ARG676

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site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE COA C1824

Chain	Residue
C	ARG676

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site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE COA D1821

Chain	Residue
D	VAL675
D	ARG676

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P19096

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_FI3
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

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

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site_id	SWS_FT_FI4
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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