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5FFI

[2Fe:2S] ferredoxin FeSII from Azotobacter vinelandii

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0009399biological_processnitrogen fixation
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0005737cellular_componentcytoplasm
B0009399biological_processnitrogen fixation
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0005737cellular_componentcytoplasm
C0009399biological_processnitrogen fixation
C0046872molecular_functionmetal ion binding
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0005737cellular_componentcytoplasm
D0009399biological_processnitrogen fixation
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
E0005737cellular_componentcytoplasm
E0009399biological_processnitrogen fixation
E0046872molecular_functionmetal ion binding
E0051536molecular_functioniron-sulfur cluster binding
E0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue FES A 1001
ChainResidue
AGLU41
ACYS42
AGLY45
ACYS47
AGLY48
ASER49
ACYS50
ACYS102

site_idAC2
Number of Residues8
Detailsbinding site for residue FES B 1001
ChainResidue
BCYS42
BGLY45
BCYS47
BGLY48
BSER49
BCYS50
BCYS102
BGLU41

site_idAC3
Number of Residues6
Detailsbinding site for residue FES C 1001
ChainResidue
CCYS42
CGLY45
CCYS47
CGLY48
CCYS50
CCYS102

site_idAC4
Number of Residues6
Detailsbinding site for residue FES D 1001
ChainResidue
DCYS42
DGLY45
DCYS47
DGLY48
DCYS50
DCYS102

site_idAC5
Number of Residues7
Detailsbinding site for residue FES E 1001
ChainResidue
ECYS42
EGLY45
EASN46
ECYS47
EGLY48
ECYS50
ECYS102

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CQDGNCGSC
ChainResidueDetails
ACYS42-CYS50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:26654855
ChainResidueDetails
ACYS42
CCYS47
CCYS50
CCYS102
DCYS42
DCYS47
DCYS50
DCYS102
ECYS42
ECYS47
ECYS50
ACYS47
ECYS102
ACYS50
ACYS102
BCYS42
BCYS47
BCYS50
BCYS102
CCYS42

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PDB entries from 2024-07-17

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