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1FND

REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES

Replaces:  2FNR
Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 317
ChainResidue
AASP84
AHIS90
ALYS91
AARG93

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FAD A 315
ChainResidue
AARG93
ALEU94
ATYR95
ASER96
ACYS114
AVAL115
ALYS116
ALEU118
ATYR120
AGLY130
AVAL131
ACYS132
ASER133
ATHR172
AGLU312
ATYR314
AHOH404
AHOH406
AHOH418
AHOH423
AHOH520

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE A2P A 316
ChainResidue
ALYS116
AGLY171
AGLY203
AVAL204
APRO205
ASER234
AARG235
ALYS244
ATYR246
AGLN248
ALEU274
AGLY276
AMET277
AHOH438
AHOH444
AHOH445
AHOH535
AHOH555
AHOH560
AHOH594

site_idFAD
Number of Residues10
DetailsRESIDUES WHICH BIND FAD
ChainResidue
ALEU94
ATYR314
ATYR95
ASER96
ACYS114
ALYS116
AVAL131
ACYS132
ASER133
ATHR172

site_idPAM
Number of Residues8
DetailsRESIDUES WHICH BIND ADENOSINE-2',5'-DIPHOSPHATE
ChainResidue
ATHR57
ALYS116
ATHR172
ASER234
AARG235
ALYS244
ATYR246
AILE247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues122
DetailsDomain: {"description":"FAD-binding FR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00716","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1986412","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9852055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
ACYS272
ASER96
AGLU312

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
ATYR95

site_idMCSA1
Number of Residues5
DetailsM-CSA 506
ChainResidueDetails
ATYR95alter redox potential, steric locator
ASER96proton shuttle (general acid/base)
ACYS272alter redox potential, electrostatic stabiliser
AGLU312alter redox potential, electrostatic stabiliser, proton shuttle (general acid/base)
ATYR314alter redox potential, steric locator

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PDB entries from 2025-12-03

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