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2BMW

Ferredoxin: NADP+ Reductase Mutant With Thr 155 Replaced By Gly, Ala 160 Replaced By Thr, Leu 263 Replaced By Pro, Arg 264 Replaced By Pro and Gly 265 Replaced by Pro (T155G-A160T-L263P-R264P-G265P)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1305
ChainResidue
ASER223
AARG224
AARG233
ATYR235
AHOH2585
AHOH2586

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD A 1304
ChainResidue
ASER80
ACYS98
AVAL99
AARG100
ALEU102
ATYR104
ALYS105
AGLY115
AVAL116
ACYS117
ASER118
ATHR160
AGLU301
ATYR303
AHOH2212
AHOH2266
AHOH2280
AHOH2573
AHOH2578
AHOH2579
AHOH2580
AHOH2583
AARG77
ALEU78
ATYR79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues124
DetailsDomain: {"description":"FAD-binding FR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00716","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsBinding site: {}
ChainResidueDetails

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
ASER80
ACYS261
AGLU301

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
ATYR79

246905

PDB entries from 2025-12-31

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