3GNC

Crystal structure of Glutaryl-COA dehydrogenase from Burkholderia Pseudomallei with fragment 6421

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000062	molecular_function	fatty-acyl-CoA binding
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0004361	molecular_function	glutaryl-CoA dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
A	0046872	molecular_function	metal ion binding
A	0046949	biological_process	fatty-acyl-CoA biosynthetic process
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000062	molecular_function	fatty-acyl-CoA binding
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0004361	molecular_function	glutaryl-CoA dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
B	0046872	molecular_function	metal ion binding
B	0046949	biological_process	fatty-acyl-CoA biosynthetic process
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0000062	molecular_function	fatty-acyl-CoA binding
C	0003995	molecular_function	acyl-CoA dehydrogenase activity
C	0004361	molecular_function	glutaryl-CoA dehydrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
C	0046872	molecular_function	metal ion binding
C	0046949	biological_process	fatty-acyl-CoA biosynthetic process
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0000062	molecular_function	fatty-acyl-CoA binding
D	0003995	molecular_function	acyl-CoA dehydrogenase activity
D	0004361	molecular_function	glutaryl-CoA dehydrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
D	0046872	molecular_function	metal ion binding
D	0046949	biological_process	fatty-acyl-CoA biosynthetic process
D	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 396

Chain	Residue
A	LYS331
A	ARG332
A	CYS335
A	ASN371
A	HIS380
A	HOH424
A	HOH442

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE QQQ A 397

Chain	Residue
A	SER101
A	LEU216
A	LEU250
A	ILE257
A	VAL370
A	TYR373
A	GLU374
A	HOH408
A	ARG97
A	SER98

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE QQQ B 396

Chain	Residue
B	ARG97
B	SER98
B	SER101
B	LEU216
B	ILE257
B	VAL370
B	TYR373
B	GLU374
B	HOH425

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE QQQ C 396

Chain	Residue
C	ARG97
C	SER98
C	SER101
C	LEU216
C	LEU250
C	ILE257
C	VAL370
C	TYR373
C	GLU374
C	HOH409

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE QQQ D 396

Chain	Residue
D	ARG97
D	SER98
D	SER101
D	LEU216
D	ILE257
D	VAL370
D	TYR373
D	GLU374
D	HOH428

---

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EPE D 397

Chain	Residue
B	LYS295
B	ASP347
D	LYS331
D	ARG332
D	CYS335
D	GLY336
D	ASN371
D	ASP378
D	HIS380
D	HOH411
D	HOH449

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE C 397

Chain	Residue
C	LYS331
C	ARG332
C	CYS335
C	ASN371
C	ASP378
C	HIS380
C	HOH406
C	HOH410

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE B 397

Chain	Residue
B	LYS331
B	ARG332
B	CYS335
B	ASN371
B	ASP378
B	HIS380
B	HOH403
B	HOH442

---

Functional Information from PROSITE/UniProt

site_id	PS00073
Number of Residues	20
Details	ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. DmLGGnGIsdEfgvaRhlvN

Chain	Residue	Details
A	ASP347-ASN366

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