Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WD9

CRYSTAL STRUCTURE OF HUMAN ACYL-COA SYNTHETASE MEDIUM-CHAIN FAMILY MEMBER 2A (L64P MUTATION) IN COMPLEX WITH IBUPROFEN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004321	molecular_function	fatty-acyl-CoA synthase activity
A	0005524	molecular_function	ATP binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006637	biological_process	acyl-CoA metabolic process
A	0015645	molecular_function	fatty acid ligase activity
A	0016405	molecular_function	CoA-ligase activity
A	0016874	molecular_function	ligase activity
A	0016878	molecular_function	acid-thiol ligase activity
A	0018858	molecular_function	benzoate-CoA ligase activity
A	0031956	molecular_function	medium-chain fatty acid-CoA ligase activity
A	0036112	biological_process	medium-chain fatty-acyl-CoA metabolic process
A	0042593	biological_process	glucose homeostasis
A	0046872	molecular_function	metal ion binding
A	0047760	molecular_function	obsolete butyrate-CoA ligase activity
A	0070328	biological_process	triglyceride homeostasis
A	0102391	molecular_function	decanoate-CoA ligase activity
B	0004321	molecular_function	fatty-acyl-CoA synthase activity
B	0005524	molecular_function	ATP binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006637	biological_process	acyl-CoA metabolic process
B	0015645	molecular_function	fatty acid ligase activity
B	0016405	molecular_function	CoA-ligase activity
B	0016874	molecular_function	ligase activity
B	0016878	molecular_function	acid-thiol ligase activity
B	0018858	molecular_function	benzoate-CoA ligase activity
B	0031956	molecular_function	medium-chain fatty acid-CoA ligase activity
B	0036112	biological_process	medium-chain fatty-acyl-CoA metabolic process
B	0042593	biological_process	glucose homeostasis
B	0046872	molecular_function	metal ion binding
B	0047760	molecular_function	obsolete butyrate-CoA ligase activity
B	0070328	biological_process	triglyceride homeostasis
B	0102391	molecular_function	decanoate-CoA ligase activity
C	0004321	molecular_function	fatty-acyl-CoA synthase activity
C	0005524	molecular_function	ATP binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0006637	biological_process	acyl-CoA metabolic process
C	0015645	molecular_function	fatty acid ligase activity
C	0016405	molecular_function	CoA-ligase activity
C	0016874	molecular_function	ligase activity
C	0016878	molecular_function	acid-thiol ligase activity
C	0018858	molecular_function	benzoate-CoA ligase activity
C	0031956	molecular_function	medium-chain fatty acid-CoA ligase activity
C	0036112	biological_process	medium-chain fatty-acyl-CoA metabolic process
C	0042593	biological_process	glucose homeostasis
C	0046872	molecular_function	metal ion binding
C	0047760	molecular_function	obsolete butyrate-CoA ligase activity
C	0070328	biological_process	triglyceride homeostasis
C	0102391	molecular_function	decanoate-CoA ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	MET483
B	HIS485
B	VAL488

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 601

Chain	Residue
C	MET483
C	HIS485
C	VAL488

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE IBP A 1570

Chain	Residue
A	GLY362
A	GLN363
A	THR364
A	GLY470
A	ARG472
A	ILE266
A	LEU267
A	VAL337

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IBP B 1570

Chain	Residue
B	ILE266
B	LEU267
B	GLY362
B	THR364
B	GLY470
B	ARG472
B	HOH2087

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IBP C 1570

Chain	Residue
C	TRP265
C	ILE266
C	GLY362
C	GLN363
C	THR364
C	GLY470
C	ARG472

Functional Information from PROSITE/UniProt

site_id	PS00455
Number of Residues	12
Details	AMP_BINDING Putative AMP-binding domain signature. IYFTSGTSGlPK

Chain	Residue	Details
A	ILE218-LYS229

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	BINDING: BINDING => ECO:0000269\|PubMed:19345228

Chain	Residue	Details
A	TYR540
B	GLN139
B	THR364
B	SER469
B	ARG472
B	ARG501
B	LYS532
B	TYR540
C	GLN139
C	THR364
C	SER469
C	ARG472
C	ARG501
C	LYS532
C	TYR540
A	GLN139
A	THR364
A	SER469
A	ARG472
A	ARG501
A	LYS532

site_id	SWS_FT_FI2
Number of Residues	15
Details	BINDING: BINDING => ECO:0000269\|PubMed:19345228, ECO:0000269\|Ref.7

Chain	Residue	Details
B	LYS557
C	THR221
C	GLU359
C	ASP446
C	ARG461
C	LYS557
A	THR221
A	GLU359
A	ASP446
A	ARG461
A	LYS557
B	THR221
B	GLU359
B	ASP446
B	ARG461

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q68CK6

Chain	Residue	Details
A	SER513
B	SER513
C	SER513

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)