Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1KQF

FORMATE DEHYDROGENASE N FROM E. COLI

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	0016491	molecular_function	oxidoreductase activity
A	0043546	molecular_function	molybdopterin cofactor binding
A	0045333	biological_process	cellular respiration
A	0047111	molecular_function	formate dehydrogenase (cytochrome-c-553) activity
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0005886	cellular_component	plasma membrane
B	0006788	biological_process	heme oxidation
B	0009055	molecular_function	electron transfer activity
B	0009061	biological_process	anaerobic respiration
B	0009326	cellular_component	formate dehydrogenase complex
B	0015944	biological_process	formate oxidation
B	0016020	cellular_component	membrane
B	0019645	biological_process	anaerobic electron transport chain
B	0036397	molecular_function	formate dehydrogenase (quinone) activity
B	0045333	biological_process	cellular respiration
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
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
C	0006788	biological_process	heme oxidation
C	0008863	molecular_function	formate dehydrogenase (NAD+) activity
C	0009055	molecular_function	electron transfer activity
C	0009061	biological_process	anaerobic respiration
C	0009326	cellular_component	formate dehydrogenase complex
C	0015944	biological_process	formate oxidation
C	0016020	cellular_component	membrane
C	0019645	biological_process	anaerobic electron transport chain
C	0020037	molecular_function	heme binding
C	0022904	biological_process	respiratory electron transport chain
C	0036397	molecular_function	formate dehydrogenase (quinone) activity
C	0045333	biological_process	cellular respiration
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 6MO A 1016

Chain	Residue
A	SEC196
A	MGD1018
A	MGD1019
A	HOH1052

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 A 1017

Chain	Residue
A	CYS92
A	LYS94
A	GLY95
A	VAL239
A	CYS50
A	TYR52
A	CYS53
A	GLY56
A	CYS57

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 805

Chain	Residue
B	CYS39
B	ILE40
B	GLY41
B	CYS42
B	LYS43
B	CYS45
B	MET80
B	CYS179
B	ILE184

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 B 806

Chain	Residue
B	LYS32
B	CYS49
B	ASN53
B	THR78
B	LYS97
B	CYS160
B	THR161
B	LEU162
B	CYS163
B	PRO173
B	CYS175

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 807

Chain	Residue
B	CYS100
B	MET101
B	CYS103
B	GLY107
B	CYS108
B	CYS143
B	PRO144
B	LYS159

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 B 808

Chain	Residue
B	CYS112
B	PRO113
B	SER114
B	ILE118
B	CYS133
B	ILE134
B	CYS136
B	GLY137
B	CYS139
B	VAL157

site_id	AC7
Number of Residues	36
Details	BINDING SITE FOR RESIDUE MGD A 1018

Chain	Residue
A	TYR101
A	GLN192
A	SEC196
A	LEU410
A	GLN414
A	HIS448
A	GLY556
A	PHE557
A	ASN558
A	SER562
A	ILE582
A	ASP583
A	PRO584
A	LEU585
A	THR587
A	SER616
A	THR617
A	ASP649
A	THR894
A	ARG896
A	HIS902
A	THR903
A	TRP904
A	ASN989
A	TYR1005
A	LYS1006
A	6MO1016
A	MGD1019
A	HOH1029
A	HOH1032
A	HOH1041
A	HOH1145
A	HOH1147
A	HOH1172
A	HOH1174
A	HOH1263

site_id	AC8
Number of Residues	36
Details	BINDING SITE FOR RESIDUE MGD A 1019

Chain	Residue
A	GLY278
A	ASP280
A	ALA409
A	LEU410
A	GLY411
A	HIS415
A	GLY447
A	HIS448
A	THR893
A	TYR895
A	ARG896
A	LEU897
A	THR898
A	HIS900
A	PHE901
A	HIS902
A	HIS975
A	LYS1006
A	6MO1016
A	MGD1018
A	HOH1031
A	HOH1046
A	HOH1085
A	HOH1138
A	LYS94
A	SEC196
A	GLY230
A	GLY231
A	ASN232
A	GLU235
A	ALA236
A	ASP259
A	PRO260
A	ARG261
A	THR263
A	SER277

site_id	AC9
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM C 809

Chain	Residue
B	TYR138
B	TRP253
C	PHE25
C	VAL28
C	ALA29
C	GLY32
C	PHE35
C	PHE36
C	ARG54
C	HIS57
C	PRO58
C	GLY61
C	ILE62
C	ILE124
C	LEU127
C	LEU128
C	GLY131
C	ILE134
C	HIS155
C	ALA156
C	HOH436
C	HOH446
C	HOH561

site_id	BC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM C 810

Chain	Residue
C	ARG9
C	HIS18
C	TRP19
C	VAL21
C	VAL22
C	PHE25
C	PHE75
C	ASN79
C	TYR109
C	GLN113
C	ILE166
C	HIS169
C	MET170
C	SER179
C	MET183
C	HOH1294
C	HOH1729

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CDL C 812

Chain	Residue
B	ASN15
B	SER16
B	ILE17
B	PRO259
B	ALA262
B	ILE266
B	HOH960
C	PHE37
C	PRO38
C	THR39
C	PHE47
C	MET170
C	HOH1083
C	HOH1150
C	HOH1263

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCGyCIaGCP

Chain	Residue	Details
B	CYS133-PRO144

site_id	PS00551
Number of Residues	19
Details	MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. NtCty.CSVgCgLlMyslgD

Chain	Residue	Details
A	ASN48-ASP66

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

Chain	Residue	Details
A	ALA927-THR954

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	63
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	5
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Non-standard residue: {"description":"Selenocysteine"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	114
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	28
Details	Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	32
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	29
Details	Domain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	31
Details	Domain: {"description":"4Fe-4S ferredoxin-type 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11884747","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	30
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	76
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details

Chain	Residue	Details
A	HIS197
A	CSE196
C	HIS169

site_id	CSA2
Number of Residues	3
Details

Chain	Residue	Details
A	HIS197
A	CSE196
C	HIS169

site_id	MCSA1
Number of Residues	1
Details	M-CSA 563

Chain	Residue	Details
C	HIS169	hydrogen bond donor, proton acceptor, proton donor, single electron acceptor, single electron donor, single electron relay
A	HIS197

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)