1H21
A novel iron centre in the split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774
Replaces: 1DDCFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009061 | biological_process | anaerobic respiration |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0009061 | biological_process | anaerobic respiration |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0009061 | biological_process | anaerobic respiration |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0009061 | biological_process | anaerobic respiration |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEC A 1248 |
| Chain | Residue |
| A | SER208 |
| B | HIS246 |
| B | PRO247 |
| A | CYS209 |
| A | CYS212 |
| A | HIS213 |
| A | TRP222 |
| A | HIS233 |
| A | HEC1249 |
| B | LYS242 |
| B | PHE243 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC A 1249 |
| Chain | Residue |
| A | CYS209 |
| A | HIS213 |
| A | GLY225 |
| A | MET227 |
| A | ASP228 |
| A | CYS229 |
| A | CYS232 |
| A | HIS233 |
| A | HEC1248 |
| B | HIS148 |
| B | ILE149 |
| B | SER152 |
| B | LYS153 |
| B | TYR156 |
| B | PRO231 |
| B | ALA238 |
| B | HEC1249 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEC B 1248 |
| Chain | Residue |
| A | TYR156 |
| A | ALA237 |
| A | ALA238 |
| A | LYS242 |
| A | HIS246 |
| A | PRO247 |
| B | CYS209 |
| B | CYS212 |
| B | HIS213 |
| B | ALA220 |
| B | HIS233 |
| B | HEC1249 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC B 1249 |
| Chain | Residue |
| A | HIS148 |
| A | ILE149 |
| A | SER152 |
| A | LYS153 |
| A | TYR156 |
| A | ALA238 |
| A | HEC1249 |
| B | CYS209 |
| B | HIS213 |
| B | MET214 |
| B | GLY225 |
| B | MET227 |
| B | ASP228 |
| B | CYS229 |
| B | CYS232 |
| B | HIS233 |
| B | HEC1248 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC C 1248 |
| Chain | Residue |
| C | CYS209 |
| C | HIS213 |
| C | MET214 |
| C | GLY225 |
| C | MET227 |
| C | ASP228 |
| C | CYS229 |
| C | CYS232 |
| C | HIS233 |
| D | HIS148 |
| D | ILE149 |
| D | SER152 |
| D | LYS153 |
| D | TYR156 |
| D | PRO231 |
| D | ALA238 |
| D | HEC1248 |
| D | HEC1250 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC D 1248 |
| Chain | Residue |
| B | LYS23 |
| B | LEU24 |
| B | ASP25 |
| C | CYS209 |
| C | CYS212 |
| C | HIS213 |
| C | ALA220 |
| C | HIS233 |
| C | HEC1248 |
| D | TYR156 |
| D | ALA237 |
| D | ALA238 |
| D | LYS242 |
| D | PHE243 |
| D | HIS246 |
| D | PRO247 |
| D | HOH2052 |
| D | HOH2053 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC D 1249 |
| Chain | Residue |
| C | PRO247 |
| D | SER208 |
| D | CYS209 |
| D | CYS212 |
| D | HIS213 |
| D | TRP222 |
| D | HIS233 |
| D | HEC1250 |
| C | TYR156 |
| C | ALA237 |
| C | ALA238 |
| C | LYS242 |
| C | PHE243 |
| C | HIS246 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC D 1250 |
| Chain | Residue |
| C | HIS148 |
| C | ILE149 |
| C | SER152 |
| C | LYS153 |
| C | TYR156 |
| C | PRO231 |
| C | ALA238 |
| C | HEC1248 |
| D | CYS209 |
| D | HIS213 |
| D | GLY225 |
| D | MET227 |
| D | ASP228 |
| D | CYS229 |
| D | CYS232 |
| D | HIS233 |
| D | HEC1249 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"axial binding residue; in chain B","evidences":[{"source":"PubMed","id":"12589573","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H21","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"covalent; in chain A","evidences":[{"source":"PubMed","id":"12589573","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H21","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"axial binding residue; in chain A","evidences":[{"source":"PubMed","id":"12589573","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H21","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"12589573","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H21","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
