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1DOI

2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI

Functional Information from GO Data
ChainGOidnamespacecontents
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_id22
Number of Residues4
DetailsFE2S2 IRON-SULFUR REDOX CENTER.
ChainResidue
ACYS63
ACYS68
ACYS71
ACYS102

site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 201
ChainResidue
AASP12
AASP31
AHOH418

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 202
ChainResidue
AASP107
AHOH274
AHOH426
AASP81
AGLN85

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 203
ChainResidue
ASER28
AMET30
AHOH374

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 204
ChainResidue
ACYS71
AALA72
ATHR101
ATYR115
AASN116
AHOH211

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 205
ChainResidue
AGLU94
AASN97
AHOH214
AHOH439
AHOH440

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 206
ChainResidue
ATHR2
AASP109
AGLU110

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 129
ChainResidue
ASER62
ACYS63
AARG64
AGLY66
AALA67
ACYS68
ACYS71
ACYS102

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGACANC
ChainResidueDetails
ACYS63-CYS71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:8612076
ChainResidueDetails
AARG64
AALA69
AALA72
AILE103

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PDB entries from 2024-07-31

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