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1FRR

CRYSTAL STRUCTURE OF [2FE-2S] FERREDOXIN I FROM EQUISETUM ARVENSE AT 1.8 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0009507cellular_componentchloroplast
A0022900biological_processelectron transport chain
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0009055molecular_functionelectron transfer activity
B0009507cellular_componentchloroplast
B0022900biological_processelectron transport chain
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 96
ChainResidue
ASER37
ACYS38
AARG39
AGLY41
AALA42
ACYS43
ACYS46
ACYS76

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES B 96
ChainResidue
BCYS38
BARG39
BGLY41
BALA42
BCYS43
BCYS46
BCYS76
BSER37

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGACSSC
ChainResidueDetails
ACYS38-CYS46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues180
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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