8RR0

CryoEM structure of Molybdenum bispyranopterin guanine dinucleotide formate dehydrogenases ForCE1 from Bacillus subtilis

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0009326	cellular_component	formate dehydrogenase complex
A	0015944	biological_process	formate oxidation
B	0003954	molecular_function	NADH dehydrogenase activity
B	0005515	molecular_function	protein binding
B	0009326	cellular_component	formate dehydrogenase complex
B	0015944	biological_process	formate oxidation
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0022904	biological_process	respiratory electron transport chain
B	0036397	molecular_function	formate dehydrogenase (quinone) activity
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0005515	molecular_function	protein binding
C	0009326	cellular_component	formate dehydrogenase complex
C	0015944	biological_process	formate oxidation
D	0003954	molecular_function	NADH dehydrogenase activity
D	0005515	molecular_function	protein binding
D	0009326	cellular_component	formate dehydrogenase complex
D	0015944	biological_process	formate oxidation
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0022904	biological_process	respiratory electron transport chain
D	0036397	molecular_function	formate dehydrogenase (quinone) 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
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0005515	molecular_function	protein binding
E	0009326	cellular_component	formate dehydrogenase complex
E	0015944	biological_process	formate oxidation
F	0003954	molecular_function	NADH dehydrogenase activity
F	0005515	molecular_function	protein binding
F	0009326	cellular_component	formate dehydrogenase complex
F	0015944	biological_process	formate oxidation
F	0016020	cellular_component	membrane
F	0016491	molecular_function	oxidoreductase activity
F	0022904	biological_process	respiratory electron transport chain
F	0036397	molecular_function	formate dehydrogenase (quinone) activity
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0005515	molecular_function	protein binding
G	0009326	cellular_component	formate dehydrogenase complex
G	0015944	biological_process	formate oxidation
H	0003954	molecular_function	NADH dehydrogenase activity
H	0005515	molecular_function	protein binding
H	0009326	cellular_component	formate dehydrogenase complex
H	0015944	biological_process	formate oxidation
H	0016020	cellular_component	membrane
H	0016491	molecular_function	oxidoreductase activity
H	0022904	biological_process	respiratory electron transport chain
H	0036397	molecular_function	formate dehydrogenase (quinone) activity
H	0046872	molecular_function	metal ion binding
H	0051536	molecular_function	iron-sulfur cluster binding
H	0051537	molecular_function	2 iron, 2 sulfur cluster binding
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding

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. CvSCGhCStVCP

Chain	Residue	Details
B	CYS191-PRO202

---

site_id	PS01337
Number of Residues	9
Details	ODC_AZ Ornithine decarboxylase antizyme signature. TLEYAEEKT

Chain	Residue	Details
B	THR515-THR523

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	160
Details	Domain: {"description":"4Fe-4S His(Cys)3-ligated-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	124
Details	Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	116
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	224
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_FI5
Number of Residues	64
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---