3AGA
Crystal structure of RCC-bound red chlorophyll catabolite reductase from Arabidopsis thaliana
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE RCC A 1000 |
| Chain | Residue |
| A | ILE135 |
| A | SER287 |
| A | ILE288 |
| A | ASP291 |
| A | LEU292 |
| A | PHE316 |
| A | SER139 |
| A | PHE141 |
| A | GLU154 |
| A | ILE156 |
| A | TYR207 |
| A | SER209 |
| A | VAL214 |
| A | PHE218 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 1 |
| Chain | Residue |
| A | LEU199 |
| A | LEU201 |
| A | VAL204 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RCC B 1000 |
| Chain | Residue |
| B | ILE135 |
| B | SER139 |
| B | PHE141 |
| B | GLU154 |
| B | ILE156 |
| B | TYR207 |
| B | SER209 |
| B | PRO210 |
| B | PHE218 |
| B | SER287 |
| B | ASP291 |
| B | PHE316 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 2 |
| Chain | Residue |
| B | HOH22 |
| B | LEU199 |
| B | LYS200 |
| B | LEU201 |
| B | VAL204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 62 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20727901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AGA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AGC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for stereospecificity of the product","evidences":[{"source":"PubMed","id":"20727901","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
