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1QJD

Flavocytochrome C3 from Shewanella frigidimarina

Functional Information from GO Data
ChainGOidnamespacecontents
A0008202biological_processsteroid metabolic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEC A 1569
ChainResidue
AVAL9
AHOH2564
ACYS14
ACYS17
AHIS18
ALEU24
ASER73
AALA74
AHIS75
AHOH2563

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEC A 1570
ChainResidue
ALEU4
APHE7
AHIS8
AGLN12
ASER16
AGLN35
ACYS36
ACYS39
AHIS40
AHIS72
ATYR94
AHEC1571
AHOH2565

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEC A 1571
ChainResidue
AHIS40
ALEU43
AHIS52
AALA57
AHIS58
AVAL66
AALA67
ACYS68
ACYS71
AHIS72
APHE90
AASN91
AMET92
AHEC1570
AHOH2134
AHOH2566
AHOH2567

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEC A 1572
ChainResidue
AHIS54
ATYR55
AASN56
ASER60
AHIS61
APHE62
ACYS82
ASER84
ACYS85
AHIS86
APHE88
ALEU167
AVAL374
ALYS431
ALYS434
ATYR435
AHOH2238
AHOH2469
AHOH2571
AHOH2572
AHOH2573
AHOH2574

site_idAC5
Number of Residues44
DetailsBINDING SITE FOR RESIDUE FAD A 1573
ChainResidue
AILE553
ATEO1574
AHOH2365
AHOH2539
AHOH2540
AHOH2575
AHOH2576
AVAL132
AGLY133
AGLY135
AGLY136
AALA137
AGLU156
ALYS157
AGLU158
AGLY162
AGLY163
AASN164
AALA165
ALEU167
AALA168
AALA169
AGLY170
AGLY171
ATHR276
AARG277
AGLY278
AALA312
ATHR313
AGLY314
ATHR336
AASN337
AGLN338
AASP344
AMET375
AHIS504
AHIS505
AGLY533
AGLU534
AARG544
AGLY547
AASN548
AALA549
AILE550

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TEO A 1574
ChainResidue
AALA169
AGLY170
AMET236
AHIS365
ATHR377
AGLU378
AARG402
AHIS504
AARG544
AGLY546
AGLY547
AFAD1573

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1575
ChainResidue
ATHR506
AMET507
AGLY508
AGLU534
ATHR536
AHOH2523

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1576
ChainResidue
ALYS371
AGLU454
AHOH2471
AHOH2519

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 Residues5
DetailsBINDING: covalent => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
AASN11
ALEU43
AVAL46
AALA57
ASER60

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: covalent => ECO:0000250|UniProtKB:P83223
ChainResidueDetails
ACYS14
ACYS36
ACYS17
ACYS39
ACYS68
ACYS71
ACYS82
ACYS85

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
AASP15
AASN33
AALA47
ATHR50

site_idSWS_FT_FI5
Number of Residues17
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
AASP27
ATHR146
AVAL253
ATHR313
ASER406
APHE480
AGLY509
AGLN524
AVAL525
ATHR49
AVAL66
ATHR69
ALYS112
AVAL131
APHE139
ASER140
ASER144

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P83223
ChainResidueDetails
AHIS61
AHIS8
AHIS18
AHIS40
AHIS58
AHIS72
AHIS75
AHIS86

site_idSWS_FT_FI7
Number of Residues27
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P83223
ChainResidueDetails
AALA145
AALA137
AGLU156
AASN164
AALA169
AGLY170
AGLY171
AGLY278
AASP344
ATYR361
AHIS365
AGLY340
AGLU378
AHIS504
AHIS505
AGLU534
AARG544
AGLY547
AALA549
AILE550
AALA352
AGLY353
ATHR377
AASP479
AMET519
ALYS522
AALA74

site_idSWS_FT_FI8
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0C278
ChainResidueDetails
AARG402

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

site_idMCSA1
Number of Residues7
DetailsM-CSA 20
ChainResidueDetails
AHIS365increase acidity
AGLU378proton acceptor, proton donor, proton relay
AARG381proton acceptor, proton donor, proton relay
AARG402proton acceptor, proton donor
AHIS504electrostatic stabiliser, proton acceptor, proton donor
AHIS505electrostatic stabiliser
AARG544steric role

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PDB entries from 2024-07-24

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