1M64
Crystal structure of Q363F mutant flavocytochrome c3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009061 | biological_process | anaerobic respiration |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019645 | biological_process | anaerobic electron transport chain |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009061 | biological_process | anaerobic respiration |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019645 | biological_process | anaerobic electron transport chain |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 3002 |
| Chain | Residue |
| A | THR506 |
| A | MET507 |
| A | GLY508 |
| A | GLU534 |
| A | THR536 |
| A | HOH3009 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 4002 |
| Chain | Residue |
| B | GLU534 |
| B | THR536 |
| B | HOH4016 |
| B | THR506 |
| B | MET507 |
| B | GLY508 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM A 801 |
| Chain | Residue |
| A | CYS14 |
| A | CYS17 |
| A | HIS18 |
| A | SER73 |
| A | ALA74 |
| A | HIS75 |
| A | HOH3142 |
| A | HOH3235 |
| A | HOH3276 |
| A | HOH3343 |
| A | HOH3834 |
| A | HOH3905 |
| A | HOH3970 |
| A | HOH4063 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 802 |
| Chain | Residue |
| A | LEU4 |
| A | PHE7 |
| A | HIS8 |
| A | GLN12 |
| A | SER16 |
| A | GLN35 |
| A | CYS36 |
| A | CYS39 |
| A | HIS40 |
| A | HIS72 |
| A | TYR94 |
| A | HEM803 |
| A | HOH3102 |
| A | HOH3362 |
| A | HOH3564 |
| A | HOH3684 |
| A | HOH3903 |
| A | HOH3913 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 803 |
| Chain | Residue |
| A | HIS40 |
| A | LEU43 |
| A | VAL46 |
| A | HIS52 |
| A | ALA57 |
| A | HIS58 |
| A | ALA67 |
| A | CYS68 |
| A | CYS71 |
| A | HIS72 |
| A | PHE90 |
| A | ASN91 |
| A | MET92 |
| A | HEM802 |
| A | HOH3025 |
| A | HOH3359 |
| A | HOH3398 |
| A | HOH3728 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 804 |
| Chain | Residue |
| A | HIS54 |
| A | ASN56 |
| A | SER60 |
| A | HIS61 |
| A | PHE62 |
| A | CYS82 |
| A | SER84 |
| A | CYS85 |
| A | HIS86 |
| A | PHE88 |
| A | LEU167 |
| A | VAL374 |
| A | LYS431 |
| A | LYS434 |
| A | HOH3064 |
| A | HOH3079 |
| A | HOH3085 |
| A | HOH3113 |
| A | HOH3118 |
| A | HOH3149 |
| A | HOH3508 |
| A | HOH3520 |
| site_id | AC7 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE FAD A 3000 |
| Chain | Residue |
| A | GLY170 |
| A | GLY171 |
| A | ARG277 |
| A | GLY278 |
| A | ALA312 |
| A | THR313 |
| A | GLY314 |
| A | THR336 |
| A | ASN337 |
| A | GLN338 |
| A | ASP344 |
| A | MET375 |
| A | HIS504 |
| A | HIS505 |
| A | GLY533 |
| A | GLU534 |
| A | GLY547 |
| A | ASN548 |
| A | ALA549 |
| A | ILE550 |
| A | ILE553 |
| A | FUM3001 |
| A | HOH3010 |
| A | HOH3011 |
| A | HOH3017 |
| A | HOH3022 |
| A | HOH3050 |
| A | VAL132 |
| A | GLY133 |
| A | GLY135 |
| A | GLY136 |
| A | ALA137 |
| A | GLU156 |
| A | LYS157 |
| A | GLU158 |
| A | GLY162 |
| A | GLY163 |
| A | ASN164 |
| A | ALA165 |
| A | LEU167 |
| A | ALA168 |
| A | ALA169 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FUM A 3001 |
| Chain | Residue |
| A | GLY170 |
| A | HIS365 |
| A | MET375 |
| A | THR377 |
| A | GLU378 |
| A | HIS504 |
| A | ARG544 |
| A | GLY546 |
| A | GLY547 |
| A | FAD3000 |
| A | HOH3066 |
| A | HOH3130 |
| A | HOH3290 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM B 801 |
| Chain | Residue |
| B | CYS14 |
| B | CYS17 |
| B | HIS18 |
| B | LEU24 |
| B | SER73 |
| B | ALA74 |
| B | HIS75 |
| B | HOH4181 |
| B | HOH4244 |
| B | HOH4362 |
| B | HOH4647 |
| B | HOH4739 |
| B | HOH4979 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM B 802 |
| Chain | Residue |
| B | HIS8 |
| B | GLN12 |
| B | CYS36 |
| B | CYS39 |
| B | HIS40 |
| B | HIS72 |
| B | TYR94 |
| B | HEM803 |
| B | HOH4365 |
| B | HOH4370 |
| B | HOH4390 |
| B | HOH4497 |
| B | HOH4731 |
| B | HOH4966 |
| site_id | BC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 803 |
| Chain | Residue |
| B | HIS40 |
| B | LEU43 |
| B | HIS52 |
| B | ALA57 |
| B | HIS58 |
| B | VAL66 |
| B | CYS68 |
| B | CYS71 |
| B | HIS72 |
| B | PHE90 |
| B | ASN91 |
| B | MET92 |
| B | HEM802 |
| B | HOH4065 |
| B | HOH4306 |
| B | HOH4497 |
| B | HOH4532 |
| B | HOH4954 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 804 |
| Chain | Residue |
| B | HIS54 |
| B | ASN56 |
| B | SER60 |
| B | HIS61 |
| B | PHE62 |
| B | CYS82 |
| B | SER84 |
| B | CYS85 |
| B | HIS86 |
| B | PHE88 |
| B | LEU167 |
| B | VAL374 |
| B | LYS431 |
| B | LYS434 |
| B | HOH4074 |
| B | HOH4112 |
| B | HOH4123 |
| B | HOH4149 |
| B | HOH4297 |
| B | HOH4323 |
| B | HOH4485 |
| site_id | BC4 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE FAD B 4000 |
| Chain | Residue |
| B | VAL132 |
| B | GLY133 |
| B | GLY135 |
| B | GLY136 |
| B | ALA137 |
| B | GLU156 |
| B | LYS157 |
| B | GLU158 |
| B | GLY162 |
| B | GLY163 |
| B | ASN164 |
| B | ALA165 |
| B | LEU167 |
| B | ALA168 |
| B | ALA169 |
| B | GLY170 |
| B | GLY171 |
| B | ARG277 |
| B | GLY278 |
| B | ALA312 |
| B | THR313 |
| B | GLY314 |
| B | THR336 |
| B | GLN338 |
| B | ASP344 |
| B | MET375 |
| B | HIS504 |
| B | HIS505 |
| B | GLY533 |
| B | GLU534 |
| B | GLY547 |
| B | ASN548 |
| B | ALA549 |
| B | ILE550 |
| B | ILE553 |
| B | FUM4001 |
| B | HOH4005 |
| B | HOH4007 |
| B | HOH4009 |
| B | HOH4011 |
| B | HOH4014 |
| site_id | BC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FUM B 4001 |
| Chain | Residue |
| B | GLY170 |
| B | HIS365 |
| B | THR377 |
| B | GLU378 |
| B | HIS504 |
| B | ARG544 |
| B | GLY546 |
| B | GLY547 |
| B | FAD4000 |
| B | HOH4110 |
| B | HOH4175 |
| B | HOH4254 |
Functional Information from PROSITE/UniProt
| site_id | PS00028 |
| Number of Residues | 23 |
| Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cvs..ChgtLaevaettkHehynaH |
| Chain | Residue | Details |
| A | CYS36-HIS58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:10978153 |
| Chain | Residue | Details |
| A | THR377 | |
| B | THR377 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39 |
| Chain | Residue | Details |
| A | HIS8 | |
| B | HIS18 | |
| B | ASP15 | |
| B | ASN33 | |
| B | CYS36 | |
| B | ALA47 | |
| B | THR50 | |
| B | HIS61 | |
| A | HIS18 | |
| A | ASP15 | |
| A | ASN33 | |
| A | CYS36 | |
| A | ALA47 | |
| A | THR50 | |
| A | HIS61 | |
| B | HIS8 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: covalent => ECO:0007744|PDB:1E39 |
| Chain | Residue | Details |
| A | CYS14 | |
| B | CYS14 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: covalent => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39 |
| Chain | Residue | Details |
| A | CYS17 | |
| B | VAL46 | |
| B | ALA57 | |
| B | SER60 | |
| A | ASN11 | |
| A | LEU43 | |
| A | VAL46 | |
| A | ALA57 | |
| A | SER60 | |
| B | CYS17 | |
| B | ASN11 | |
| B | LEU43 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10978153, ECO:0007744|PDB:1E39 |
| Chain | Residue | Details |
| A | ASP27 | |
| A | THR146 | |
| A | VAL253 | |
| A | THR313 | |
| A | THR377 | |
| A | SER406 | |
| A | PHE480 | |
| A | GLY509 | |
| A | GLN524 | |
| A | VAL525 | |
| B | ASP27 | |
| A | THR49 | |
| B | THR49 | |
| B | VAL66 | |
| B | THR69 | |
| B | LYS112 | |
| B | VAL131 | |
| B | PHE139 | |
| B | SER140 | |
| B | SER144 | |
| B | THR146 | |
| B | VAL253 | |
| A | VAL66 | |
| B | THR313 | |
| B | THR377 | |
| B | SER406 | |
| B | PHE480 | |
| B | GLY509 | |
| B | GLN524 | |
| B | VAL525 | |
| A | THR69 | |
| A | LYS112 | |
| A | VAL131 | |
| A | PHE139 | |
| A | SER140 | |
| A | SER144 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P83223 |
| Chain | Residue | Details |
| A | ALA145 | |
| B | ALA352 | |
| B | GLY353 | |
| B | ASP479 | |
| B | MET519 | |
| B | LYS522 | |
| A | GLY340 | |
| A | ALA352 | |
| A | GLY353 | |
| A | ASP479 | |
| A | MET519 | |
| A | LYS522 | |
| B | ALA145 | |
| B | GLY340 |
