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3AV8

Refined Structure of Plant-type [2Fe-2S] Ferredoxin I from Aphanothece sacrum at 1.46 A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0022900biological_processelectron transport chain
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0009055molecular_functionelectron transfer activity
B0022900biological_processelectron transport chain
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0009055molecular_functionelectron transfer activity
C0022900biological_processelectron transport chain
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0009055molecular_functionelectron transfer activity
D0022900biological_processelectron transport chain
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES A 98
ChainResidue
ASER38
ACYS39
AARG40
AGLY42
AALA43
ACYS44
ACYS47
ALEU76
ACYS78

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 99
ChainResidue
BLYS50
BTYR74
BLYS92
BALA95
BHOH316
DHOH124
DHOH195
DHOH280

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES B 98
ChainResidue
BSER38
BCYS39
BARG40
BGLY42
BALA43
BCYS44
BCYS47
BCYS78

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES C 98
ChainResidue
CSER38
CCYS39
CARG40
CGLY42
CALA43
CCYS44
CCYS47
CCYS78

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 C 99
ChainResidue
APRO55
AGLY84
AASP85
AHOH184
AHOH268
CALA1
CASP20
CHOH151
CHOH263

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES D 98
ChainResidue
DSER38
DCYS39
DARG40
DGLY42
DALA43
DCYS44
DCYS47
DCYS78

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGACSTC
ChainResidueDetails
ACYS39-CYS47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:2123937
ChainResidueDetails
ACYS39
CCYS44
CCYS47
CCYS78
DCYS39
DCYS44
DCYS47
DCYS78
ACYS44
ACYS47
ACYS78
BCYS39
BCYS44
BCYS47
BCYS78
CCYS39

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PDB entries from 2024-09-04

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