Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1H0H

Tungsten containing Formate Dehydrogenase from Desulfovibrio Gigas

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008863	molecular_function	formate dehydrogenase (NAD+) activity
A	0009055	molecular_function	electron transfer activity
A	0009061	biological_process	anaerobic respiration
A	0016491	molecular_function	oxidoreductase activity
A	0030151	molecular_function	molybdenum ion binding
A	0042597	cellular_component	periplasmic space
A	0043546	molecular_function	molybdopterin cofactor binding
A	0045333	biological_process	cellular respiration
A	0046872	molecular_function	metal ion binding
A	0047111	molecular_function	formate dehydrogenase (cytochrome-c-553) activity
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
K	0008863	molecular_function	formate dehydrogenase (NAD+) activity
K	0009055	molecular_function	electron transfer activity
K	0009061	biological_process	anaerobic respiration
K	0016491	molecular_function	oxidoreductase activity
K	0030151	molecular_function	molybdenum ion binding
K	0042597	cellular_component	periplasmic space
K	0043546	molecular_function	molybdopterin cofactor binding
K	0045333	biological_process	cellular respiration
K	0046872	molecular_function	metal ion binding
K	0047111	molecular_function	formate dehydrogenase (cytochrome-c-553) activity
K	0051536	molecular_function	iron-sulfur cluster binding
K	0051539	molecular_function	4 iron, 4 sulfur cluster binding
L	0042597	cellular_component	periplasmic space
L	0046872	molecular_function	metal ion binding
L	0051536	molecular_function	iron-sulfur cluster binding
L	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 1100

Chain	Residue
A	THR358
A	LYS360
A	LYS363
A	LEU393
A	GLY394
A	ASN395
A	HOH2328

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA K 1100

Chain	Residue
K	LYS363
K	LEU393
K	GLY394
K	ASN395
K	HOH2287
K	THR358
K	LYS360

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE W A 1000

Chain	Residue
A	SEC158
A	2MD1001
A	MGD1002
A	UNX1003

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE W K 1000

Chain	Residue
K	SEC158
K	2MD1001
K	MGD1002
K	UNX1003

site_id	AC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE 2MD A 1001

Chain	Residue
A	ALA130
A	GLN154
A	ILE157
A	SEC158
A	MET371
A	GLU409
A	GLY516
A	GLN517
A	ASN518
A	SER522
A	VAL542
A	ASN543
A	ILE544
A	CYS572
A	ALA573
A	LYS578
A	ASP605
A	THR854
A	ARG856
A	GLN862
A	THR863
A	LEU865
A	MET866
A	TRP936
A	ASN951
A	THR967
A	W1000
A	MGD1002
A	UNX1003
A	HOH2646
A	HOH2692
A	HOH2697

site_id	AC6
Number of Residues	34
Details	BINDING SITE FOR RESIDUE MGD A 1002

Chain	Residue
A	LYS56
A	SEC158
A	GLY192
A	SER193
A	ASN194
A	GLU197
A	ASN198
A	VAL219
A	ASP220
A	PRO221
A	ARG222
A	SER238
A	GLY239
A	ASP241
A	ALA370
A	MET371
A	TRP373
A	GLY408
A	TYR855
A	ARG856
A	VAL857
A	THR858
A	HIS860
A	TRP861
A	GLN862
A	HIS937
A	LYS968
A	W1000
A	2MD1001
A	UNX1003
A	HOH2053
A	HOH2317
A	HOH2700
A	HOH2701

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE UNX A 1003

Chain	Residue
A	SEC158
A	GLU409
A	VAL412
A	W1000
A	2MD1001
A	MGD1002

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 A 1010

Chain	Residue
A	CYS54
A	GLY57
A	PRO200
A	ILE201
A	CYS17
A	TYR19
A	CYS20
A	CYS24
A	LEU53

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE A 1200

Chain	Residue
A	HOH2702
A	HOH2703
A	HOH2704
B	PRO42
B	ASP43
B	ASP123
B	ARG126
B	TYR211

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 1011

Chain	Residue
B	CYS11
B	THR12
B	ALA13
B	CYS14
B	ARG15
B	CYS17
B	CYS156
B	THR158
B	MET161

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 B 1012

Chain	Residue
B	PHE4
B	CYS21
B	HIS25
B	GLN71
B	CYS137
B	ASP138
B	MET139
B	CYS140
B	PRO150
B	CYS152

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 1013

Chain	Residue
B	CYS72
B	ARG73
B	CYS75
B	PRO79
B	CYS80
B	CYS120
B	TYR122
B	PRO125
B	LYS136

site_id	BC4
Number of Residues	32
Details	BINDING SITE FOR RESIDUE 2MD K 1001

Chain	Residue
K	ALA130
K	GLN154
K	ILE157
K	SEC158
K	MET371
K	GLU409
K	GLY516
K	GLN517
K	ASN518
K	SER522
K	VAL542
K	ASN543
K	ILE544
K	CYS572
K	ALA573
K	LYS578
K	ASP605
K	THR854
K	ARG856
K	GLN862
K	THR863
K	LEU865
K	MET866
K	TRP936
K	ASN951
K	THR967
K	W1000
K	MGD1002
K	UNX1003
K	HOH2561
K	HOH2611
K	HOH2618

site_id	BC5
Number of Residues	35
Details	BINDING SITE FOR RESIDUE MGD K 1002

Chain	Residue
K	LYS56
K	SEC158
K	GLY192
K	SER193
K	ASN194
K	GLU197
K	ASN198
K	VAL219
K	ASP220
K	PRO221
K	ARG222
K	SER238
K	GLY239
K	ASP241
K	ALA370
K	MET371
K	TRP373
K	GLY408
K	TYR855
K	ARG856
K	VAL857
K	THR858
K	HIS860
K	TRP861
K	GLN862
K	HIS937
K	LYS968
K	W1000
K	2MD1001
K	UNX1003
K	HOH2162
K	HOH2276
K	HOH2612
K	HOH2619
K	HOH2620

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE UNX K 1003

Chain	Residue
K	SEC158
K	GLU409
K	VAL412
K	W1000
K	2MD1001
K	MGD1002

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 K 1010

Chain	Residue
K	CYS17
K	TYR19
K	CYS20
K	GLY23
K	CYS24
K	LEU53
K	CYS54
K	LYS56
K	GLY57
K	PRO200
K	ILE201

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EPE K 1200

Chain	Residue
K	HOH2623
L	PRO42
L	ASP43
L	ASP123

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 L 1011

Chain	Residue
L	CYS11
L	THR12
L	ALA13
L	CYS14
L	ARG15
L	CYS17
L	CYS156
L	THR158
L	MET161

site_id	CC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 L 1012

Chain	Residue
L	PHE4
L	CYS21
L	HIS25
L	LYS50
L	GLN71
L	CYS137
L	ASP138
L	MET139
L	CYS140
L	PRO150
L	CYS152

site_id	CC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 L 1013

Chain	Residue
L	CYS72
L	ARG73
L	CYS75
L	PRO79
L	CYS80
L	CYS120
L	TYR122
L	PRO125
L	LYS136

Functional Information from PROSITE/UniProt

site_id	PS00551
Number of Residues	19
Details	MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. SvCcy.CSVgCgLiVhtdkK

Chain	Residue	Details
A	SER15-LYS33

site_id	PS00932
Number of Residues	28
Details	MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AtlrGIkNgDkViLeSvrGklwakAiIT

Chain	Residue	Details
A	ALA889-THR916

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	116
Details	Domain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12220497","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H0H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12220497","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PDB","id":"1H0H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Non-standard residue: {"description":"Selenocysteine","evidences":[{"source":"PubMed","id":"12220497","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	58
Details	Domain: {"description":"4Fe-4S ferredoxin-type 1"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	78
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11372198","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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