2DGE
Crystal structure of oxidized cytochrome C6A from Arabidopsis thaliana
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0020037 | molecular_function | heme binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0020037 | molecular_function | heme binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | ASP74 |
| A | GLU159 |
| C | ASP74 |
| C | LYS155 |
| C | GLU159 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1002 |
| Chain | Residue |
| D | GLU159 |
| B | ASP74 |
| B | GLU159 |
| D | ASP74 |
| D | LYS155 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 200 |
| Chain | Residue |
| A | CYS86 |
| A | CYS89 |
| A | HIS90 |
| A | ASN95 |
| A | ALA101 |
| A | THR102 |
| A | LEU103 |
| A | ASP107 |
| A | LEU108 |
| A | ASN111 |
| A | THR123 |
| A | LYS127 |
| A | MET130 |
| A | HOH1005 |
| A | HOH1010 |
| A | HOH1025 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM B 200 |
| Chain | Residue |
| B | ALA85 |
| B | CYS86 |
| B | CYS89 |
| B | HIS90 |
| B | ASN95 |
| B | ILE97 |
| B | GLN98 |
| B | ALA101 |
| B | THR102 |
| B | LEU103 |
| B | ASP107 |
| B | LEU108 |
| B | ASN111 |
| B | VAL113 |
| B | THR123 |
| B | LYS127 |
| B | MET130 |
| B | PHE133 |
| B | HOH1009 |
| B | HOH1020 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM C 200 |
| Chain | Residue |
| A | ARG110 |
| A | HOH1002 |
| C | ALA85 |
| C | CYS86 |
| C | CYS89 |
| C | HIS90 |
| C | ASN95 |
| C | ALA101 |
| C | THR102 |
| C | LEU103 |
| C | ASP107 |
| C | LEU108 |
| C | ASN111 |
| C | VAL113 |
| C | THR123 |
| C | LYS127 |
| C | MET130 |
| C | PHE133 |
| C | HOH223 |
| D | GLY88 |
| D | ILE96 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM D 200 |
| Chain | Residue |
| B | ARG110 |
| B | HOH1012 |
| B | HOH1038 |
| C | ILE96 |
| D | ALA85 |
| D | CYS86 |
| D | CYS89 |
| D | HIS90 |
| D | ASN95 |
| D | ALA101 |
| D | THR102 |
| D | LEU103 |
| D | ASP107 |
| D | LEU108 |
| D | ASN111 |
| D | VAL113 |
| D | THR123 |
| D | LYS127 |
| D | MET130 |
| D | PHE133 |
| D | HOH207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16777100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16815443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17625855","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
