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2VYQ

FERREDOXIN:NADP REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR, LEU 263 REPLACED BY PRO AND TYR 303 REPLACED BY SER (T155G-A160T-L263P-Y303S)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FAD A 304
ChainResidue
AARG77
ALYS105
AGLY115
AVAL116
ACYS117
ASER118
ATHR160
AGLU301
ASER303
AHOH2177
AHOH2225
ALEU78
AHOH2287
AHOH2479
AHOH2480
AHOH2481
AHOH2482
AHOH2483
AHOH2486
ATYR79
ASER80
ACYS98
AVAL99
AARG100
ALEU102
ATYR104

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
ASER223
AARG224
AARG233
ATYR235
AHOH2487
AHOH2488

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 306
ChainResidue
ALEU31
AARG163
ATYR201
AGLU204
AHOH2331
AHOH2490

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
APHE170
ALYS171
AASP172
AILE208
ATYR212
AHOH2295
AHOH2491

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

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PDB entries from 2025-08-27

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