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4H4X

Crystal Structure of Ferredoxin reductase, BphA4 E175A/T176R/Q177G mutant (oxidized form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 501
ChainResidue
AGLY14
ASER52
ALYS53
AVAL80
AALA82
AALA108
ATHR109
AGLY110
AARG130
AILE156
AGLY272
AGLY16
AASP273
AGLU289
ATHR290
ATRP291
AALA294
ATYR319
ATRP320
AHOH601
AHOH603
AHOH606
ALEU17
AHOH608
AHOH609
AHOH626
AHOH648
AHOH669
AHOH682
AHOH687
AALA18
AVAL38
AASP40
AGLU41
AARG48
APRO49

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
APRO113
ATHR128
ALEU129
AVAL233
AGLY234
AILE235
AGLY236
AFMT508
AHOH628

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 503
ChainResidue
AALA115
ALEU116
AHOH891
AHOH906

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 504
ChainResidue
AVAL217
AARG225
ATRP320
AHOH662
AHOH860

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 505
ChainResidue
ATHR109
AASN240
AASP241
AALA242
ALEU243
AALA244
AHOH648

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 506
ChainResidue
AASP54
APHE55
AHIS58
AGLY59
AASP60
AASP215

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 507
ChainResidue
AALA122
ATHR123
AMET124
ASER213
AVAL214
AASP215
AGLY216

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 508
ChainResidue
AVAL155
AILE156
AGOL502
AHOH737
AHOH750
AHOH773

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 509
ChainResidue
AARG327
AASN369
AASN370
AALA371
AHOH832
AHOH877

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 510
ChainResidue
AALA162
ATYR196
AHIS197
AGLN200
AVAL202
AHOH870

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PDB entries from 2024-09-04

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