Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1FFV

CARBON MONOXIDE DEHYDROGENASE FROM HYDROGENOPHAGA PSEUDOFLAVA

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	0043885	molecular_function	anaerobic carbon-monoxide dehydrogenase 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	0043885	molecular_function	anaerobic carbon-monoxide dehydrogenase 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	7
Details	BINDING SITE FOR RESIDUE FES A 1907

Chain	Residue
A	GLN100
A	CYS101
A	GLY102
A	CYS104
A	CYS136
A	ARG137
A	CYS138

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES A 1908

Chain	Residue
A	SER45
A	HIS46
A	CYS47
A	GLY48
A	CYS50
A	LYS60
A	CYS62
A	GLY41
A	CYS42

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES D 1909

Chain	Residue
D	GLN100
D	CYS101
D	GLY102
D	CYS104
D	CYS136
D	ARG137
D	CYS138

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES D 1910

Chain	Residue
D	GLY41
D	CYS42
D	SER45
D	HIS46
D	CYS47
D	GLY48
D	CYS50
D	LYS60
D	CYS62

site_id	AC5
Number of Residues	38
Details	BINDING SITE FOR RESIDUE PCD B 1920

Chain	Residue
A	GLN100
A	CYS138
B	GLN237
B	GLY266
B	GLY267
B	PHE268
B	GLY269
B	ALA382
B	TYR383
B	ARO384
B	CSZ385
B	GLN522
B	GLY523
B	GLN524
B	HIS526
B	THR529
B	TYR562
B	GLY563
B	SER564
B	ARG565
B	SER566
B	THR567
B	CYS680
B	THR682
B	ILE684
B	ASN685
B	ILE688
B	ILE689
B	GLN692
B	LYS753
B	GLY754
B	VAL755
B	ALA756
B	GLU757
B	HOH2240
B	HOH2389
B	HOH2390
B	HOH2391

site_id	AC6
Number of Residues	39
Details	BINDING SITE FOR RESIDUE PCD E 1921

Chain	Residue
E	LYS753
E	GLY754
E	VAL755
E	ALA756
E	GLU757
E	HOH2087
E	HOH2188
E	HOH2355
E	HOH2367
E	HOH2414
D	GLN100
D	CYS138
E	GLN237
E	GLY266
E	GLY267
E	PHE268
E	GLY269
E	ALA382
E	TYR383
E	ARO384
E	CSZ385
E	GLN522
E	GLY523
E	GLN524
E	HIS526
E	THR529
E	THR561
E	TYR562
E	GLY563
E	SER564
E	ARG565
E	SER566
E	THR567
E	CYS680
E	THR682
E	ILE684
E	ASN685
E	ILE689
E	GLN692

site_id	AC7
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD C 1922

Chain	Residue
A	SER45
A	HIS46
C	LYS29
C	LEU30
C	ALA32
C	GLY33
C	GLY34
C	HIS35
C	SER36
C	LEU37
C	ILE101
C	ALA102
C	GLY110
C	THR111
C	GLY114
C	ASP115
C	ALA117
C	HIS118
C	ASN123
C	ASP124
C	LEU161
C	VAL166
C	MET167
C	LYS185
C	GLY191
C	ASP192
C	TRP193
C	HOH1981
C	HOH2007
C	HOH2024
C	HOH2046

site_id	AC8
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD F 1923

Chain	Residue
D	SER45
F	LYS29
F	LEU30
F	ALA32
F	GLY33
F	GLY34
F	HIS35
F	SER36
F	LEU37
F	ILE54
F	ILE101
F	ALA102
F	GLY110
F	THR111
F	GLY114
F	ASP115
F	ALA117
F	ASN123
F	ASP124
F	LEU161
F	VAL166
F	MET167
F	LYS185
F	GLY191
F	ASP192
F	TRP193
F	HOH1961
F	HOH1967
F	HOH2013
F	HOH2017

Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DAKLLAGGHSL

Chain	Residue	Details
C	ASP27-LEU37

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	152
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	36
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"4-hydroxyarginine","evidences":[{"source":"PubMed","id":"10966817","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	352
Details	Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
B	GLU757

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
E	GLU757

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
B	GLN237

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
E	GLN237

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