Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7Z0T

Structure of the Escherichia coli formate hydrogenlyase complex (aerobic preparation, composite structure)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003954	molecular_function	NADH dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006007	biological_process	glucose catabolic process
A	0008863	molecular_function	formate dehydrogenase (NAD+) activity
A	0009061	biological_process	anaerobic respiration
A	0009326	cellular_component	formate dehydrogenase complex
A	0015942	biological_process	formate metabolic process
A	0015944	biological_process	formate oxidation
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
A	0019628	biological_process	urate catabolic process
A	0019645	biological_process	anaerobic electron transport chain
A	0043546	molecular_function	molybdopterin cofactor binding
A	0045272	cellular_component	obsolete plasma membrane respiratory chain complex I
A	0045333	biological_process	cellular respiration
A	0046872	molecular_function	metal ion binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	1990204	cellular_component	oxidoreductase complex
B	0006007	biological_process	glucose catabolic process
B	0009061	biological_process	anaerobic respiration
B	0009326	cellular_component	formate dehydrogenase complex
B	0015944	biological_process	formate oxidation
B	0019645	biological_process	anaerobic electron transport chain
B	0046872	molecular_function	metal ion binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0005886	cellular_component	plasma membrane
C	0006007	biological_process	glucose catabolic process
C	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
C	0009061	biological_process	anaerobic respiration
C	0009326	cellular_component	formate dehydrogenase complex
C	0015944	biological_process	formate oxidation
C	0016491	molecular_function	oxidoreductase activity
C	0019645	biological_process	anaerobic electron transport chain
C	0042773	biological_process	ATP synthesis coupled electron transport
C	1902600	biological_process	proton transmembrane transport
D	0005886	cellular_component	plasma membrane
D	0006007	biological_process	glucose catabolic process
D	0009061	biological_process	anaerobic respiration
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	0019645	biological_process	anaerobic electron transport chain
E	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
E	0016151	molecular_function	nickel cation binding
E	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
E	0048038	molecular_function	quinone binding
E	0051287	molecular_function	NAD binding
F	0003954	molecular_function	NADH dehydrogenase activity
F	0006007	biological_process	glucose catabolic process
F	0009060	biological_process	aerobic respiration
F	0009061	biological_process	anaerobic respiration
F	0009326	cellular_component	formate dehydrogenase complex
F	0015944	biological_process	formate oxidation
F	0016020	cellular_component	membrane
F	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
F	0019645	biological_process	anaerobic electron transport chain
F	0046872	molecular_function	metal ion binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0005515	molecular_function	protein binding
G	0006007	biological_process	glucose catabolic process
G	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
G	0009061	biological_process	anaerobic respiration
G	0009326	cellular_component	formate dehydrogenase complex
G	0015944	biological_process	formate oxidation
G	0016491	molecular_function	oxidoreductase activity
G	0019645	biological_process	anaerobic electron transport chain
G	0046872	molecular_function	metal ion binding
G	0048038	molecular_function	quinone binding
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	1902600	biological_process	proton transmembrane transport

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. CiGCAaCVnACP

Chain	Residue	Details
F	CYS40-PRO51
F	CYS75-PRO86
B	CYS82-PRO93

site_id	PS00490
Number of Residues	18
Details	MOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TkTAsaADVILPsTSwgE

Chain	Residue	Details
A	THR433-GLU450

site_id	PS00535
Number of Residues	12
Details	COMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. VHRGmEKLaEtR

Chain	Residue	Details
E	VAL216-ARG227

site_id	PS00551
Number of Residues	18
Details	MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. TvCpy.CASgCkInLvvd.N

Chain	Residue	Details
A	THR6-ASN23

site_id	PS00667
Number of Residues	16
Details	COMPLEX1_ND1_1 Respiratory-chain NADH dehydrogenase subunit 1 signature 1. GVLQeYrDIIKLLgRQ

Chain	Residue	Details
D	GLY38-GLN53

site_id	PS00668
Number of Residues	14
Details	COMPLEX1_ND1_2 Respiratory-chain NADH dehydrogenase subunit 1 signature 2. PFDLAEAEq.ELqeG

Chain	Residue	Details
D	PRO194-GLY207

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

Chain	Residue	Details
A	ALA615-SER642

site_id	PS01150
Number of Residues	17
Details	COMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GtDKIVPVDVYiPgCPP

Chain	Residue	Details
G	GLY131-PRO147

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Electron donor/acceptor

Chain	Residue	Details
A	LYS44
B	CYS85
B	CYS88
B	CYS92
B	CYS143
B	CYS146
B	CYS155
B	CYS159
D	SER89-GLN93
D	GLY153-TRP167
D	GLY243-LEU253
D	ALA306-ALA307
F	CYS78
F	CYS81
F	CYS85
B	CYS82

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor

Chain	Residue	Details
A	SEC140
D	PRO68-GLY88
D	LEU94-SER114
D	MET132-ALA152
D	PRO168-ILE188
D	TRP222-TRP242
D	LEU254-PHE274
D	ILE285-LEU305

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01004, ECO:0000269\|PubMed:16830149, ECO:0000269\|PubMed:9036855

Chain	Residue	Details
A	CYS8
A	TYR10
A	CYS11
A	CYS15
A	CYS42

site_id	SWS_FT_FI4
Number of Residues	11
Details	BINDING: BINDING => ECO:0000269\|PubMed:16830149, ECO:0000269\|PubMed:9036855

Chain	Residue	Details
A	LYS44
A	TYR678
A	LYS679
A	MET297
A	GLN301
A	GLN335
A	SER445
A	ASP478
A	CYS588
A	TYR654
A	GLN655

site_id	SWS_FT_FI5
Number of Residues	10
Details	BINDING:

Chain	Residue	Details
A	ARG110
A	CYS661
A	SEC140
A	PHE173
A	CYS201
A	GLY221
A	GLY402
A	GLN428
A	THR579
A	ARG581

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Important for catalytic activity

Chain	Residue	Details
A	HIS141
A	ARG333

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 562

Chain	Residue	Details
A	LYS44	electrostatic stabiliser
A	SEC140	electrophile, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
A	HIS141	electrostatic stabiliser, proton acceptor
A	ARG333	electrostatic stabiliser, hydrogen bond donor

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