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1JRY

Crystal structure of Arg402Lys mutant flavocytochrome c3 from Shewanella frigidimarina

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
B0008202biological_processsteroid metabolic process
B0009055molecular_functionelectron transfer activity
B0009061biological_processanaerobic respiration
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0019645biological_processanaerobic electron transport chain
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046872molecular_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
AHOH1067

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 2810
ChainResidue
BGLU534
BTHR536
BHOH2847
BTHR506
BMET507
BGLY508

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 801
ChainResidue
AHIS8
AVAL9
ACYS14
ACYS17
AHIS18
ALEU24
ATHR69
ASER73
AALA74
AHIS75
ATYR298
AHEM802
AHOH1412
AHOH1550
AHOH1633
AHOH1764
AHOH1913
AHOH2227
AHOH2328

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 802
ChainResidue
ALEU4
APHE7
AHIS8
AGLN12
ASER16
AGLN35
ACYS36
ACYS39
AHIS40
AHIS72
ATYR94
AHEM801
AHEM803
AHOH1352
AHOH1878
AHOH2163
AHOH2334
AHOH2472
AHOH2740

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 803
ChainResidue
AHIS40
ALEU43
AVAL46
ATHR49
ATHR50
AHIS52
AALA57
AHIS58
AVAL66
AALA67
ACYS68
ACYS71
AHIS72
APHE90
AASN91
AMET92
AHEM802
AHEM804
AHOH1077
AHOH1644
AHOH1890

site_idAC6
Number of Residues27
DetailsBINDING SITE FOR RESIDUE HEM A 804
ChainResidue
AHIS54
ATYR55
AASN56
ASER60
AHIS61
APHE62
ACYS82
ASER84
ACYS85
AHIS86
APHE88
ALEU167
AGLN338
AVAL374
ALYS431
ALYS434
ATYR435
ALEU438
AHEM803
AHOH1148
AHOH1181
AHOH1189
AHOH1207
AHOH1314
AHOH1506
AHOH1988
AHOH2178

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 801
ChainResidue
BVAL9
BCYS14
BCYS17
BHIS18
BLEU24
BSER73
BALA74
BHIS75
BHEM802
BHOH3053
BHOH3189
BHOH3308
BHOH3327
BHOH3331
BHOH3681
BHIS8

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 802
ChainResidue
BPHE7
BHIS8
BGLN12
BSER16
BGLN35
BCYS36
BCYS39
BHIS40
BHIS72
BPRO93
BTYR94
BHEM801
BHEM803
BHOH3193
BHOH3252
BHOH3443
BHOH3492
BHOH3597
BHOH3729

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 803
ChainResidue
BHIS40
BLEU43
BHIS52
BALA57
BHIS58
BVAL66
BALA67
BCYS68
BCYS71
BHIS72
BCYS82
BPHE90
BASN91
BMET92
BHEM802
BHEM804
BHOH2944
BHOH2964
BHOH3165
BHOH3291

site_idBC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM B 804
ChainResidue
BHIS54
BTYR55
BASN56
BSER60
BHIS61
BPHE62
BCYS82
BSER84
BCYS85
BHIS86
BPHE88
BLEU167
BGLN338
BVAL374
BLYS431
BLYS434
BTYR435
BHEM803
BHOH2873
BHOH2883
BHOH2885
BHOH2951
BHOH3061
BHOH3167
BHOH3244
BHOH3321

site_idBC2
Number of Residues44
DetailsBINDING SITE FOR RESIDUE FAD A 1805
ChainResidue
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
AILE553
AHOH1073
AHOH1081
AHOH1082
AHOH1135
AHOH1266
AFUM1806

site_idBC3
Number of Residues44
DetailsBINDING SITE FOR RESIDUE FAD B 2805
ChainResidue
BVAL132
BGLY133
BGLY135
BGLY136
BALA137
BGLU156
BLYS157
BGLU158
BGLY162
BGLY163
BASN164
BALA165
BLEU167
BALA168
BALA169
BGLY170
BGLY171
BTHR276
BARG277
BGLY278
BALA312
BTHR313
BGLY314
BTHR336
BGLN338
BASP344
BMET375
BHIS504
BHIS505
BGLY533
BGLU534
BARG544
BGLY547
BASN548
BALA549
BILE550
BILE553
BFUM2806
BHOH2812
BHOH2822
BHOH2850
BHOH2861
BHOH2968
BHOH3038

site_idBC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FUM A 1806
ChainResidue
AGLY170
AMET236
AHIS365
AMET375
ATHR377
AGLU378
ALYS402
AHIS504
AARG544
AGLY546
AGLY547
AFAD1805

site_idBC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FUM B 2806
ChainResidue
BGLY170
BMET236
BHIS365
BMET375
BTHR377
BGLU378
BLYS402
BHIS504
BARG544
BGLY546
BGLY547
BFAD2805

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 Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:10978153
ChainResidueDetails
ATHR377
BTHR377

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
AHIS8
BHIS18
BASP15
BASN33
BCYS36
BALA47
BTHR50
BHIS61
AHIS18
AASP15
AASN33
ACYS36
AALA47
ATHR50
AHIS61
BHIS8

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: covalent => ECO:0007744|PDB:1E39
ChainResidueDetails
ACYS14
BCYS14

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: covalent => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
ACYS17
BVAL46
BALA57
BSER60
AASN11
ALEU43
AVAL46
AALA57
ASER60
BCYS17
BASN11
BLEU43

site_idSWS_FT_FI5
Number of Residues36
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39
ChainResidueDetails
AASP27
ATHR146
AVAL253
ATHR313
ATHR377
ASER406
APHE480
AGLY509
AGLN524
AVAL525
BASP27
ATHR49
BTHR49
BVAL66
BTHR69
BLYS112
BVAL131
BPHE139
BSER140
BSER144
BTHR146
BVAL253
AVAL66
BTHR313
BTHR377
BSER406
BPHE480
BGLY509
BGLN524
BVAL525
ATHR69
ALYS112
AVAL131
APHE139
ASER140
ASER144

site_idSWS_FT_FI6
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P83223
ChainResidueDetails
AALA145
BALA352
BGLY353
BASP479
BMET519
BLYS522
AGLY340
AALA352
AGLY353
AASP479
AMET519
ALYS522
BALA145
BGLY340

219140

PDB entries from 2024-05-01

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