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9GBU

Desulfovibrio desulfuricans [FeFe]-hydrogenase variant with both subunits linked by a 13 amino acid linker peptide derived from a group A1 type [FeFe]-hydrogenase of Solobacterium moorei

Functional Information from GO Data
ChainGOidnamespacecontents
A0008901molecular_functionferredoxin hydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0008901molecular_functionferredoxin hydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCDtCSqYCP
ChainResidueDetails
ACYS35-PRO46
ACYS66-PRO77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues62
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10368269","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HFE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 127
ChainResidueDetails
AGLU156proton acceptor, proton donor, proton relay
AGLU159proton acceptor, proton donor, proton relay
ACYS178proton acceptor, proton donor, proton relay
ASER198proton acceptor, proton donor, proton relay
ALYS237proton acceptor, proton donor, proton relay
AGLU240proton acceptor, proton donor, proton relay
AGLU245proton acceptor, proton donor, proton relay
ACYS382metal ligand

site_idMCSA2
Number of Residues8
DetailsM-CSA 127
ChainResidueDetails
BGLU156proton acceptor, proton donor, proton relay
BGLU159proton acceptor, proton donor, proton relay
BCYS178proton acceptor, proton donor, proton relay
BSER198proton acceptor, proton donor, proton relay
BLYS237proton acceptor, proton donor, proton relay
BGLU240proton acceptor, proton donor, proton relay
BGLU245proton acceptor, proton donor, proton relay
BCYS382metal ligand

247536

PDB entries from 2026-01-14

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