1MOK

NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
A	0016491	molecular_function	oxidoreductase activity
A	0042208	biological_process	propylene catabolic process
A	0050628	molecular_function	2-oxopropyl-CoM reductase (carboxylating) activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
B	0016491	molecular_function	oxidoreductase activity
B	0042208	biological_process	propylene catabolic process
B	0050628	molecular_function	2-oxopropyl-CoM reductase (carboxylating) activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
C	0016491	molecular_function	oxidoreductase activity
C	0042208	biological_process	propylene catabolic process
C	0050628	molecular_function	2-oxopropyl-CoM reductase (carboxylating) activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
D	0016491	molecular_function	oxidoreductase activity
D	0042208	biological_process	propylene catabolic process
D	0050628	molecular_function	2-oxopropyl-CoM reductase (carboxylating) activity
D	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD A 524

Chain	Residue
A	GLY50
A	ALA86
A	CYS87
A	HIS90
A	HIS91
A	PRO157
A	ALA158
A	ALA181
A	VAL182
A	HIS202
A	THR225
A	GLY52
A	TYR229
A	GLY352
A	ASP353
A	MET359
A	GLU360
A	MET361
A	ALA364
A	PHE390
B	PHE501
A	ALA53
A	ALA54
A	ASP73
A	ARG74
A	TRP75
A	GLY80
A	SER81

---

site_id	AC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD B 524

Chain	Residue
A	PHE501
B	GLY50
B	GLY51
B	ALA53
B	ALA54
B	ASP73
B	ARG74
B	TRP75
B	GLY80
B	SER81
B	ALA86
B	CYS87
B	HIS90
B	HIS91
B	PRO157
B	ALA158
B	ALA181
B	VAL182
B	GLY183
B	HIS202
B	THR225
B	GLU314
B	GLY352
B	ASP353
B	MET359
B	GLU360
B	MET361
B	ALA364

---

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FAD C 524

Chain	Residue
C	GLY50
C	ALA53
C	ALA54
C	ASP73
C	ARG74
C	TRP75
C	GLY80
C	SER81
C	ALA86
C	CYS87
C	HIS90
C	HIS91
C	PRO157
C	ALA158
C	ALA181
C	VAL182
C	GLY183
C	HIS202
C	THR225
C	TYR229
C	GLY352
C	ASP353
C	MET359
C	GLU360
C	MET361
D	PHE501

---

site_id	AC4
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD D 524

Chain	Residue
D	ALA181
D	VAL182
D	HIS202
D	THR225
D	TYR229
D	GLY352
D	ASP353
D	MET359
D	GLU360
D	MET361
D	ALA364
D	PHE390
C	PHE501
D	GLY50
D	GLY52
D	ALA53
D	ALA54
D	VAL72
D	ASP73
D	ARG74
D	TRP75
D	GLY80
D	SER81
D	ALA86
D	CYS87
D	HIS90
D	HIS91
D	PRO157
D	ALA158

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:12390015, ECO:0000269|PubMed:16388586, ECO:0000269|PubMed:21192936, ECO:0007744|PDB:1MO9, ECO:0007744|PDB:1MOK, ECO:0007744|PDB:2C3C, ECO:0007744|PDB:2C3D, ECO:0007744|PDB:3Q6J

Chain	Residue	Details
A	MET361
A	PHE501
B	ALA53
B	SER81
B	ALA158
B	ASP353
B	MET361
B	PHE501
C	ALA53
C	SER81
C	ALA158
C	ASP353
C	MET361
C	PHE501
D	ALA53
D	SER81
D	ALA158
D	ASP353
D	MET361
D	PHE501
A	ALA53
A	SER81
A	ALA158
A	ASP353

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:12390015, ECO:0000269|PubMed:21192936, ECO:0000305|PubMed:16388586, ECO:0007744|PDB:1MO9, ECO:0007744|PDB:3Q6J

Chain	Residue	Details
A	ARG56
A	ARG365
B	ARG56
B	ARG365
C	ARG56
C	ARG365
D	ARG56
D	ARG365

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:21192936, ECO:0000305|PubMed:16388586, ECO:0007744|PDB:3Q6J

Chain	Residue	Details
A	CYS82
B	CYS82
C	CYS82
D	CYS82

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:16388586, ECO:0000269|PubMed:21192936, ECO:0007744|PDB:2C3C, ECO:0007744|PDB:3Q6J

Chain	Residue	Details
A	GLY222
A	ARG245
A	GLU360
B	GLY222
B	ARG245
B	GLU360
C	GLY222
C	ARG245
C	GLU360
D	GLY222
D	ARG245
D	GLU360

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 378

Chain	Residue	Details
A	LEU78	electrostatic stabiliser, modifies pKa
A	CYS82	covalent catalysis
A	CYS87	covalent catalysis
A	HIS137	modifies pKa
A	PHE501	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 378

Chain	Residue	Details
B	LEU78	electrostatic stabiliser, modifies pKa
B	CYS82	covalent catalysis
B	CYS87	covalent catalysis
B	HIS137	modifies pKa
B	PHE501	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 378

Chain	Residue	Details
C	LEU78	electrostatic stabiliser, modifies pKa
C	CYS82	covalent catalysis
C	CYS87	covalent catalysis
C	HIS137	modifies pKa
C	PHE501	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	5
Details	M-CSA 378

Chain	Residue	Details
D	LEU78	electrostatic stabiliser, modifies pKa
D	CYS82	covalent catalysis
D	CYS87	covalent catalysis
D	HIS137	modifies pKa
D	PHE501	electrostatic stabiliser

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