3DAY

Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in complex with AMP-CPP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0006629	biological_process	lipid metabolic process
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	butyrate-CoA ligase activity
A	0070328	biological_process	triglyceride homeostasis
A	0102391	molecular_function	decanoate-CoA ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	MET483
A	HIS485
A	HOH924
A	HOH936
A	HOH939

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 602

Chain	Residue
A	HOH791
A	HOH1361
A	HOH1362
A	HOH1411

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 603

Chain	Residue
A	ARG316
A	LEU342
A	THR345

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL A 604

Chain	Residue
A	LEU288
A	PRO289
A	LYS290
A	PHE291
A	ASP292
A	HOH694

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 605

Chain	Residue
A	ASP49
A	HIS53

---

site_id	AC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE APC A 606

Chain	Residue
A	THR221
A	SER222
A	GLY223
A	THR224
A	SER225
A	LYS229
A	GLY338
A	GLU339
A	SER340
A	GLU359
A	SER360
A	TYR361
A	GLY362
A	GLN363
A	THR364
A	ASP446
A	PHE458
A	ARG461
A	LYS557
A	HOH734
A	HOH761
A	HOH776
A	HOH791
A	HOH874
A	HOH1211
A	HOH1361
A	HOH1362
A	HOH1402
A	HOH1411

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TRS A 607

Chain	Residue
A	MET80
A	TRP81
A	GLU85
A	HOH910

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 608

Chain	Residue
A	TRP71
A	LYS77
A	LEU79
A	PRO117
A	GLU118
A	LYS195
A	HOH832
A	HOH883

---

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	7
Details	BINDING: BINDING => ECO:0000269|PubMed:19345228

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

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7

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

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q68CK6

Chain	Residue	Details
A	SER513

---