1S6V
Structure of a cytochrome c peroxidase-cytochrome c site specific cross-link
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004601 | molecular_function | peroxidase activity |
A | 0006979 | biological_process | response to oxidative stress |
A | 0020037 | molecular_function | heme binding |
A | 0034599 | biological_process | cellular response to oxidative stress |
B | 0005515 | molecular_function | protein binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005758 | cellular_component | mitochondrial intermembrane space |
B | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
B | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
B | 0009055 | molecular_function | electron transfer activity |
B | 0020037 | molecular_function | heme binding |
B | 0046872 | molecular_function | metal ion binding |
B | 1901612 | molecular_function | cardiolipin binding |
C | 0004601 | molecular_function | peroxidase activity |
C | 0006979 | biological_process | response to oxidative stress |
C | 0020037 | molecular_function | heme binding |
C | 0034599 | biological_process | cellular response to oxidative stress |
D | 0005515 | molecular_function | protein binding |
D | 0005739 | cellular_component | mitochondrion |
D | 0005758 | cellular_component | mitochondrial intermembrane space |
D | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
D | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
D | 0009055 | molecular_function | electron transfer activity |
D | 0020037 | molecular_function | heme binding |
D | 0046872 | molecular_function | metal ion binding |
D | 1901612 | molecular_function | cardiolipin binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 800 |
Chain | Residue |
A | ALA8 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEC A 296 |
Chain | Residue |
A | HIS175 |
A | LEU177 |
A | GLY178 |
A | LYS179 |
A | THR180 |
A | HIS181 |
A | ASN184 |
A | SER185 |
A | TRP191 |
A | LEU232 |
A | PRO44 |
A | THR234 |
A | HOH804 |
A | HOH812 |
A | HOH824 |
A | HOH1039 |
A | VAL45 |
A | ARG48 |
A | TRP51 |
A | PRO145 |
A | ALA147 |
A | LEU171 |
A | ALA174 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEC B 104 |
Chain | Residue |
A | ALA193 |
B | ARG13 |
B | CYS14 |
B | CYS17 |
B | HIS18 |
B | VAL28 |
B | PRO30 |
B | ILE35 |
B | SER40 |
B | GLY41 |
B | TYR46 |
B | TYR48 |
B | THR49 |
B | ASN52 |
B | TRP59 |
B | MET64 |
B | TYR67 |
B | THR78 |
B | LYS79 |
B | MET80 |
B | CYS81 |
B | PHE82 |
B | HOH156 |
site_id | AC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEC C 296 |
Chain | Residue |
C | PRO44 |
C | VAL45 |
C | TRP51 |
C | PRO145 |
C | ALA147 |
C | LEU171 |
C | ALA174 |
C | HIS175 |
C | LEU177 |
C | GLY178 |
C | LYS179 |
C | THR180 |
C | HIS181 |
C | ASN184 |
C | SER185 |
C | TRP191 |
C | LEU232 |
C | THR234 |
C | HOH307 |
C | HOH314 |
C | HOH323 |
C | HOH409 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEC D 104 |
Chain | Residue |
C | ALA193 |
D | ARG13 |
D | CYS14 |
D | CYS17 |
D | HIS18 |
D | VAL28 |
D | SER40 |
D | GLY41 |
D | TYR46 |
D | TYR48 |
D | THR49 |
D | ASN52 |
D | TRP59 |
D | MET64 |
D | TYR67 |
D | THR78 |
D | LYS79 |
D | MET80 |
D | PHE82 |
D | LEU94 |
D | HOH132 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 |
Chain | Residue | Details |
B | CYS14 | |
B | CYS17 | |
D | CYS14 | |
D | CYS17 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 |
Chain | Residue | Details |
B | HIS18 | |
B | MET80 | |
D | HIS18 | |
D | MET80 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO |
Chain | Residue | Details |
B | LYS72 | |
D | LYS72 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 |
Chain | Residue | Details |
B | LYS73 | |
D | LYS73 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | TYR153 | |
C | TYR153 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
A | ARG48 | |
A | HIS52 | |
A | ASN82 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
C | ARG48 | |
C | HIS52 | |
C | ASN82 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 709 |
Chain | Residue | Details |
A | ARG48 | electrostatic stabiliser |
A | HIS52 | electrostatic stabiliser, proton acceptor, proton donor |
A | TRP191 | single electron acceptor, single electron donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 709 |
Chain | Residue | Details |
C | ARG48 | electrostatic stabiliser |
C | HIS52 | electrostatic stabiliser, proton acceptor, proton donor |
C | TRP191 | single electron acceptor, single electron donor |