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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7Z0T

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003954molecular_functionNADH dehydrogenase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006007biological_processglucose catabolic process
A0008863molecular_functionformate dehydrogenase (NAD+) activity
A0009061biological_processanaerobic respiration
A0009326cellular_componentformate dehydrogenase complex
A0015942biological_processformate metabolic process
A0015944biological_processformate oxidation
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016903molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors
A0019628biological_processurate catabolic process
A0019645biological_processanaerobic electron transport chain
A0022904biological_processrespiratory electron transport chain
A0043546molecular_functionmolybdopterin cofactor binding
A0045333biological_processcellular respiration
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A1990204cellular_componentoxidoreductase complex
B0006007biological_processglucose catabolic process
B0009061biological_processanaerobic respiration
B0009326cellular_componentformate dehydrogenase complex
B0015944biological_processformate oxidation
B0019645biological_processanaerobic electron transport chain
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0005886cellular_componentplasma membrane
C0006007biological_processglucose catabolic process
C0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
C0009061biological_processanaerobic respiration
C0009326cellular_componentformate dehydrogenase complex
C0015944biological_processformate oxidation
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0019645biological_processanaerobic electron transport chain
C0042773biological_processATP synthesis coupled electron transport
C1902600biological_processproton transmembrane transport
D0005886cellular_componentplasma membrane
D0006007biological_processglucose catabolic process
D0009061biological_processanaerobic respiration
D0009326cellular_componentformate dehydrogenase complex
D0015944biological_processformate oxidation
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0019645biological_processanaerobic electron transport chain
E0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
E0016151molecular_functionnickel cation binding
E0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
E0048038molecular_functionquinone binding
E0051287molecular_functionNAD binding
F0003954molecular_functionNADH dehydrogenase activity
F0006007biological_processglucose catabolic process
F0009060biological_processaerobic respiration
F0009061biological_processanaerobic respiration
F0009326cellular_componentformate dehydrogenase complex
F0015944biological_processformate oxidation
F0016020cellular_componentmembrane
F0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
F0019645biological_processanaerobic electron transport chain
F0046872molecular_functionmetal ion binding
F0051536molecular_functioniron-sulfur cluster binding
F0051539molecular_function4 iron, 4 sulfur cluster binding
G0005515molecular_functionprotein binding
G0006007biological_processglucose catabolic process
G0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
G0009061biological_processanaerobic respiration
G0009326cellular_componentformate dehydrogenase complex
G0015944biological_processformate oxidation
G0016491molecular_functionoxidoreductase activity
G0019645biological_processanaerobic electron transport chain
G0046872molecular_functionmetal ion binding
G0048038molecular_functionquinone binding
G0051536molecular_functioniron-sulfur cluster binding
G0051539molecular_function4 iron, 4 sulfur cluster binding
G1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCAaCVnACP
ChainResidueDetails
FCYS40-PRO51
FCYS75-PRO86
BCYS82-PRO93
site_idPS00490
Number of Residues18
DetailsMOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TkTAsaADVILPsTSwgE
ChainResidueDetails
ATHR433-GLU450
site_idPS00535
Number of Residues12
DetailsCOMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. VHRGmEKLaEtR
ChainResidueDetails
EVAL216-ARG227
site_idPS00551
Number of Residues18
DetailsMOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. TvCpy.CASgCkInLvvd.N
ChainResidueDetails
ATHR6-ASN23
site_idPS00667
Number of Residues16
DetailsCOMPLEX1_ND1_1 Respiratory-chain NADH dehydrogenase subunit 1 signature 1. GVLQeYrDIIKLLgRQ
ChainResidueDetails
DGLY38-GLN53
site_idPS00668
Number of Residues14
DetailsCOMPLEX1_ND1_2 Respiratory-chain NADH dehydrogenase subunit 1 signature 2. PFDLAEAEq.ELqeG
ChainResidueDetails
DPRO194-GLY207
site_idPS00932
Number of Residues28
DetailsMOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AkrlGIeDeAlVwVhSrkGkiitrAqVS
ChainResidueDetails
AALA615-SER642
site_idPS01150
Number of Residues17
DetailsCOMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GtDKIVPVDVYiPgCPP
ChainResidueDetails
GGLY131-PRO147
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues387
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues59
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues59
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues32
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues24
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues59
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues29
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues55
DetailsDomain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsActive site: {"description":"Electron donor/acceptor"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues23
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16830149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IV2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16830149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IV2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16830149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IV2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsNon-standard residue: {"description":"Selenocysteine","evidences":[{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 562
ChainResidueDetails
GASP44electrostatic stabiliser
GVAL140electrophile, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
GTYR141electrostatic stabiliser, proton acceptor

239803

PDB entries from 2025-08-06

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