1SQP
Crystal Structure Analysis of Bovine Bc1 with Myxothiazol
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0046872 | molecular_function | metal ion binding |
A | 0070469 | cellular_component | respirasome |
B | 0004222 | molecular_function | metalloendopeptidase activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0006508 | biological_process | proteolysis |
B | 0046872 | molecular_function | metal ion binding |
B | 0070469 | cellular_component | respirasome |
C | 0005739 | cellular_component | mitochondrion |
C | 0005743 | cellular_component | mitochondrial inner membrane |
C | 0005750 | cellular_component | mitochondrial respiratory chain complex III |
C | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
C | 0008121 | molecular_function | ubiquinol-cytochrome-c reductase activity |
C | 0009055 | molecular_function | electron transfer activity |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0020037 | molecular_function | heme binding |
C | 0022904 | biological_process | respiratory electron transport chain |
C | 0031966 | cellular_component | mitochondrial membrane |
C | 0045275 | cellular_component | respiratory chain complex III |
C | 0046872 | molecular_function | metal ion binding |
C | 0048039 | molecular_function | ubiquinone binding |
C | 0070469 | cellular_component | respirasome |
C | 1902600 | biological_process | proton transmembrane transport |
D | 0009055 | molecular_function | electron transfer activity |
D | 0020037 | molecular_function | heme binding |
E | 0008121 | molecular_function | ubiquinol-cytochrome-c reductase activity |
E | 0016020 | cellular_component | membrane |
E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
F | 0005739 | cellular_component | mitochondrion |
F | 0005743 | cellular_component | mitochondrial inner membrane |
F | 0005750 | cellular_component | mitochondrial respiratory chain complex III |
F | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
F | 0070469 | cellular_component | respirasome |
G | 0005739 | cellular_component | mitochondrion |
G | 0005743 | cellular_component | mitochondrial inner membrane |
G | 0005750 | cellular_component | mitochondrial respiratory chain complex III |
G | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
G | 0070469 | cellular_component | respirasome |
H | 0005750 | cellular_component | mitochondrial respiratory chain complex III |
H | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
I | 0008121 | molecular_function | ubiquinol-cytochrome-c reductase activity |
J | 0005739 | cellular_component | mitochondrion |
J | 0005743 | cellular_component | mitochondrial inner membrane |
J | 0005750 | cellular_component | mitochondrial respiratory chain complex III |
J | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
J | 0070469 | cellular_component | respirasome |
K | 0005739 | cellular_component | mitochondrion |
K | 0005743 | cellular_component | mitochondrial inner membrane |
K | 0005750 | cellular_component | mitochondrial respiratory chain complex III |
K | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
K | 0070469 | cellular_component | respirasome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PEE E 197 |
Chain | Residue |
C | LEU43 |
E | ASN53 |
E | GLN57 |
E | PHE58 |
J | ASP36 |
J | PLX63 |
C | MET240 |
D | HIS200 |
D | MET204 |
D | LYS207 |
D | MET208 |
D | MET211 |
E | TYR49 |
E | ALA50 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CDL A 447 |
Chain | Residue |
A | PHE336 |
A | TRP443 |
A | LEU444 |
A | ARG445 |
A | PEE448 |
C | ARG5 |
C | ILE19 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CDL D 242 |
Chain | Residue |
C | SER29 |
C | ASN32 |
C | PHE33 |
C | LYS227 |
C | LEU230 |
C | LEU234 |
D | TYR220 |
D | LYS223 |
D | ARG224 |
G | TYR29 |
G | GLY33 |
G | ASN36 |
G | ARG40 |
G | CDL82 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CDL G 82 |
Chain | Residue |
C | SER28 |
C | SER29 |
C | TRP30 |
C | PHE33 |
C | PEE380 |
D | CDL242 |
F | GLN72 |
G | ARG40 |
G | THR41 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEE A 448 |
Chain | Residue |
A | SER439 |
A | PHE442 |
A | CDL447 |
C | HIS221 |
J | PLX63 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PEE C 380 |
Chain | Residue |
C | TRP30 |
C | TYR95 |
C | MET96 |
C | GLY99 |
C | ARG100 |
C | TYR103 |
C | TYR104 |
C | MET316 |
C | PHE325 |
C | TRP326 |
C | TYR358 |
F | GLN72 |
G | VAL48 |
G | CDL82 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PLX J 63 |
Chain | Residue |
A | ASP417 |
A | PHE442 |
A | LEU444 |
A | PEE448 |
E | TYR37 |
E | THR40 |
E | PEE197 |
J | PHE14 |
J | ARG15 |
J | THR17 |
J | PHE20 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEC C 381 |
Chain | Residue |
C | TRP31 |
C | GLY34 |
C | LEU37 |
C | HIS97 |
C | VAL98 |
C | ARG100 |
C | SER106 |
C | TRP113 |
C | GLY116 |
C | VAL117 |
C | LEU119 |
C | HIS196 |
C | LEU200 |
C | SER205 |
C | ASN206 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEC C 382 |
Chain | Residue |
C | TYR131 |
C | LEU133 |
C | PRO134 |
C | PHE179 |
C | HIS182 |
C | PHE183 |
C | PRO186 |
C | ILE189 |
C | TYR273 |
C | GLN44 |
C | GLY48 |
C | LEU49 |
C | LEU51 |
C | TYR55 |
C | ARG80 |
C | HIS83 |
C | ALA84 |
C | THR126 |
C | GLY130 |
site_id | BC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE HEC D 243 |
Chain | Residue |
D | VAL36 |
D | CYS37 |
D | CYS40 |
D | HIS41 |
D | ASN105 |
D | PRO110 |
D | TYR126 |
D | VAL127 |
D | LEU130 |
D | PHE153 |
D | ILE158 |
D | GLY159 |
D | MET160 |
D | PRO163 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES E 198 |
Chain | Residue |
E | CYS139 |
E | HIS141 |
E | LEU142 |
E | GLY143 |
E | CYS144 |
E | CYS158 |
E | CYS160 |
E | HIS161 |
E | GLY162 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MYX C 383 |
Chain | Residue |
C | MET124 |
C | PHE128 |
C | TYR131 |
C | VAL132 |
C | GLY142 |
C | ILE146 |
C | PRO270 |
C | GLU271 |
C | TYR273 |
C | PHE274 |
C | LEU294 |
Functional Information from PROSITE/UniProt
site_id | PS00143 |
Number of Residues | 24 |
Details | INSULINASE Insulinase family, zinc-binding region signature. GsryensnnlGtSHLLRLAsSlTT |
Chain | Residue | Details |
B | GLY54-THR77 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:2981208 |
Chain | Residue | Details |
F | ALA1 | |
D | GLU124 | |
C | TRP113-LEU133 | |
C | PHE178-LEU198 | |
C | ILE226-ALA246 | |
C | LEU288-HIS308 | |
C | LEU320-GLY340 | |
C | TYR347-PRO367 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D855 |
Chain | Residue | Details |
F | LYS18 | |
F | LYS82 | |
F | LYS95 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9D855 |
Chain | Residue | Details |
F | LYS77 | |
F | LYS87 |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY |
Chain | Residue | Details |
E | CYS139 | |
E | HIS141 | |
E | CYS158 | |
E | HIS161 | |
E | SER163 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040, ECO:0007744|PDB:1PP9, ECO:0007744|PDB:1SQV, ECO:0007744|PDB:2A06, ECO:0007744|PDB:2YBB |
Chain | Residue | Details |
C | HIS201 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ndo |
Chain | Residue | Details |
E | HIS161 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ndo |
Chain | Residue | Details |
A | GLU60 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ndo |
Chain | Residue | Details |
B | ARG70 |