Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1N5W

Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Oxidized form

Replaces: 1QJ2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008805	molecular_function	carbon-monoxide oxygenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0005506	molecular_function	iron ion binding
B	0005507	molecular_function	copper ion binding
B	0008805	molecular_function	carbon-monoxide oxygenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0030151	molecular_function	molybdenum ion binding
B	0043885	molecular_function	anaerobic carbon-monoxide dehydrogenase activity
B	0046872	molecular_function	metal ion binding
C	0008805	molecular_function	carbon-monoxide oxygenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0071949	molecular_function	FAD binding
D	0008805	molecular_function	carbon-monoxide oxygenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
E	0005506	molecular_function	iron ion binding
E	0005507	molecular_function	copper ion binding
E	0008805	molecular_function	carbon-monoxide oxygenase activity
E	0016491	molecular_function	oxidoreductase activity
E	0030151	molecular_function	molybdenum ion binding
E	0043885	molecular_function	anaerobic carbon-monoxide dehydrogenase activity
E	0046872	molecular_function	metal ion binding
F	0008805	molecular_function	carbon-monoxide oxygenase activity
F	0016491	molecular_function	oxidoreductase activity
F	0050660	molecular_function	flavin adenine dinucleotide binding
F	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 3001

Chain	Residue
A	HIS5
A	HOH3985
A	HOH4040
A	HOH4069
A	HOH4071
A	HOH4072

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES A 3907

Chain	Residue
A	CYS105
A	CYS137
A	ARG138
A	CYS139
A	GLN101
A	CYS102
A	GLY103

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES A 3908

Chain	Residue
A	GLY41
A	CYS42
A	SER45
A	CYS47
A	GLY48
A	CYS50
A	CYS62

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CUM B 3921

Chain	Residue
B	GLN240
B	GLY272
B	ALA385
B	TYR386
B	ARG387
B	CYS388
B	SER389
B	TYR568
B	GLY569
B	GLU763
B	MCN3920
B	HOH4334

site_id	AC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE MCN B 3920

Chain	Residue
A	GLN101
A	CYS139
B	GLY270
B	PHE271
B	ARG387
B	GLN528
B	GLY529
B	GLN530
B	HIS532
B	THR535
B	THR567
B	TYR568
B	GLY569
B	SER570
B	ARG571
B	SER572
B	THR573
B	CYS686
B	THR688
B	ILE690
B	ASN691
B	ILE694
B	ILE695
B	GLN698
B	LYS759
B	GLY760
B	VAL761
B	GLY762
B	GLU763
B	CUM3921
B	HOH3970
B	HOH4002

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES D 4907

Chain	Residue
D	GLN101
D	CYS102
D	GLY103
D	CYS105
D	CYS137
D	ARG138
D	CYS139

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES D 4908

Chain	Residue
D	GLY41
D	CYS42
D	SER45
D	HIS46
D	CYS47
D	GLY48
D	CYS50
D	CYS62

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CUM E 4921

Chain	Residue
E	GLN240
E	PHE271
E	GLY272
E	ALA385
E	TYR386
E	ARG387
E	CYS388
E	SER389
E	TYR568
E	GLY569
E	GLU763
E	MCN4920
E	HOH5313

site_id	AC9
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MCN E 4920

Chain	Residue
E	GLN530
E	HIS532
E	THR535
E	THR567
E	TYR568
E	GLY569
E	SER570
E	ARG571
E	SER572
E	THR573
E	CYS686
E	THR688
E	ILE690
E	ASN691
E	ILE694
E	ILE695
E	GLN698
E	LYS759
E	GLY760
E	VAL761
E	GLY762
E	GLU763
E	CUM4921
E	HOH5034
D	GLN101
D	CYS139
E	GLY270
E	PHE271
E	ARG387
E	GLN528
E	GLY529

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FAD F 4931

Chain	Residue
D	SER45
D	HIS46
F	HIS35
F	ILE101
F	ALA102
F	ILE106
F	ASN115
F	ASN123
F	ASP124
F	LYS185
F	GLY191
F	ASP192
F	TYR193
F	HOH4986

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE FAD C 3932

Chain	Residue
A	SER45
A	HIS46
C	HIS35
C	ILE101
C	ALA102
C	ASN115
C	ASN123
C	ASP124
C	LYS185
C	GLY191
C	ASP192
C	TYR193
C	HOH4062

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:10430865, ECO:0000269\|PubMed:12475995

Chain	Residue	Details
C	ALA32
D	CYS47
D	CYS50
D	CYS62
D	CYS102
D	CYS105
D	CYS137
D	CYS139
C	THR111
F	ALA32
F	THR111
A	CYS102
A	CYS105
A	CYS137
A	CYS139
D	CYS42

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10430865, ECO:0000269\|PubMed:12475995

Chain	Residue	Details
B	GLU763
E	GLU763

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 10430865, 10636886, 11076018

Chain	Residue	Details
B	CYS388
B	GLN240
B	ARG387

site_id	CSA2
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10430865, 10636886, 11076018

Chain	Residue	Details
H	GLN240
H	ARG387

site_id	MCSA1
Number of Residues	4
Details	M-CSA 107

Chain	Residue	Details
B	GLN240	electrostatic stabiliser
B	ARG387	electrostatic stabiliser
B	CYS388	metal ligand
B	GLU763	proton acceptor, proton donor, proton relay

site_id	MCSA2
Number of Residues	4
Details	M-CSA 107

Chain	Residue	Details
E	GLN240	electrostatic stabiliser
E	ARG387	electrostatic stabiliser
E	CYS388	metal ligand
E	GLU763	proton acceptor, proton donor, proton relay

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)