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2B7R

Structure of E378D mutant flavocytochrome c3

Functional Information from GO Data
ChainGOidnamespacecontents
A0008202biological_processsteroid metabolic process
A0009055molecular_functionelectron transfer activity
A0009061biological_processanaerobic respiration
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0019645biological_processanaerobic electron transport chain
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1810
ChainResidue
ATHR506
AMET507
AGLY508
AGLU534
ATHR536
AHOH1865

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 801
ChainResidue
ASER73
AALA74
AHIS75
AHOH2017
AHOH2022
AHOH2068
AHOH2272
AHOH2799
AHOH2800
ACYS14
ACYS17
AHIS18

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM A 802
ChainResidue
ALEU4
APHE7
AHIS8
AGLN12
ASER16
ACYS36
ACYS39
AHIS40
AHIS72
ATYR94
AHOH2277
AHOH2506
AHOH2645

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 803
ChainResidue
AHIS40
ALEU43
AHIS52
AALA57
AHIS58
AVAL66
AALA67
ACYS68
ACYS71
AHIS72
APHE90
AASN91
AMET92
AHEM804
AHOH1890
AHOH2251
AHOH2827

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 804
ChainResidue
AHIS54
AASN56
ASER60
AHIS61
ACYS82
ASER84
ACYS85
AHIS86
APHE88
ALEU167
AGLN338
AVAL374
ALYS431
ALYS434
AHEM803
AHOH1815
AHOH1830
AHOH1850
AHOH1885
AHOH1989
AHOH2004
AHOH2012
AHOH2302
AHOH2332

site_idAC6
Number of Residues42
DetailsBINDING SITE FOR RESIDUE FAD A 1805
ChainResidue
AHIS505
AGLY533
AGLU534
AARG544
AGLY547
AASN548
AALA549
AILE550
AILE553
AFUM1806
AHOH1814
AHOH1817
AHOH1818
AHOH1819
AHOH1844
AVAL132
AGLY133
AGLY135
AGLY136
AALA137
AGLU156
ALYS157
AGLU158
AGLY162
AGLY163
AASN164
AALA165
ALEU167
AALA168
AALA169
AGLY170
AGLY171
AARG277
AGLY278
AALA312
ATHR313
AGLY314
ATHR336
AGLN338
AASP344
AMET375
AHIS504

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FUM A 1806
ChainResidue
AGLY170
AHIS365
ATHR377
AASP378
AARG402
AHIS504
AARG544
AGLY546
AGLY547
AFAD1805

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues23
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cvs..ChgtLaevaettkHehynaH
ChainResidueDetails
ACYS36-HIS58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:10978153
ChainResidueDetails
ATHR377

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
AHIS8
AHIS18
AASP15
AASN33
ACYS36
AALA47
ATHR50
AHIS61

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: covalent => ECO:0007744|PDB:1E39
ChainResidueDetails
ACYS14

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: covalent => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
ACYS17
AASN11
ALEU43
AVAL46
AALA57
ASER60

site_idSWS_FT_FI5
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
AASP27
ATHR146
AVAL253
ATHR313
ATHR377
ASER406
APHE480
AGLY509
AGLN524
AVAL525
ATHR49
AVAL66
ATHR69
ALYS112
AVAL131
APHE139
ASER140
ASER144

site_idSWS_FT_FI6
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P83223
ChainResidueDetails
AALA145
AGLY340
AALA352
AGLY353
AASP479
AMET519
ALYS522

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
AHIS504
AARG544
AHIS365
AARG402

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PDB entries from 2024-07-24

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