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1P2H

H61M mutant of 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 810
ChainResidue
ATHR506
AMET507
AGLY508
AGLU534
ATHR536
AHOH852

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 801
ChainResidue
ACYS14
ACYS17
AHIS18
ALEU24
ASER73
AALA74
AHIS75
ATYR298
AHOH906
AHOH994
AHOH1121
AHOH1124
AHOH1185
AHOH1348
AALA5
AHIS8
AVAL9

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM A 802
ChainResidue
ALEU4
AHIS8
AGLN12
ASER16
ACYS36
ACYS39
AHIS40
AHIS72
ATYR94
AHEM803

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 803
ChainResidue
AHIS40
AGLY41
ALEU43
AVAL46
ATHR49
ATHR50
AHIS52
AHIS58
AVAL66
ACYS68
ACYS71
AHIS72
AVAL80
ACYS82
APHE90
AASN91
AMET92
AHEM802
AHEM804
AHOH899
AHOH905
AHOH1259

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 804
ChainResidue
AHIS54
AASN56
AALA57
ASER60
APHE62
ACYS82
ASER84
ACYS85
AHIS86
APHE88
ALEU167
AGLN338
AVAL374
ALYS431
ALYS434
ALEU438
AHEM803
AHOH831
AHOH929
AHOH958
AHOH1351

site_idAC6
Number of Residues45
DetailsBINDING SITE FOR RESIDUE FAD A 805
ChainResidue
ATHR336
AASN337
AGLN338
AASP344
AMET375
AHIS504
AHIS505
AGLY533
AGLU534
AARG544
AGLY547
AASN548
AALA549
AILE550
AILE553
ATEO806
AHOH815
AHOH820
AHOH823
AHOH844
AHOH854
AHOH862
AVAL132
AGLY133
AGLY135
AGLY136
AALA137
AGLU156
ALYS157
AGLU158
AGLY162
AGLY163
AASN164
AALA165
ALEU167
AALA168
AALA169
AGLY170
AGLY171
ATHR276
AARG277
AGLY278
AALA312
ATHR313
AGLY314

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TEO A 806
ChainResidue
AALA169
AGLY170
AMET236
AHIS365
AMET375
ATHR377
AGLU378
AARG402
AHIS504
AARG544
AGLY546
AGLY547
AFAD805

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
AMET61

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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