2X9J
Structure of the Mutant D206N of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in complex with bound substrate Biliverdin IXA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010024 | biological_process | phytochromobilin biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
| A | 7770044 | molecular_function | phycoerythrobilin synthase activity |
| B | 0010024 | biological_process | phytochromobilin biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
| B | 7770044 | molecular_function | phycoerythrobilin synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE BLA A 1234 |
| Chain | Residue |
| A | ILE79 |
| A | TYR141 |
| A | ARG142 |
| A | PHE143 |
| A | PHE144 |
| A | TYR158 |
| A | MET202 |
| A | ASN206 |
| A | PRO207 |
| A | VAL208 |
| A | TYR211 |
| A | ILE86 |
| A | HOH2218 |
| A | HOH2219 |
| A | ASN88 |
| A | ILE90 |
| A | ASP105 |
| A | MET107 |
| A | ILE115 |
| A | VAL117 |
| A | GLN121 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE BLA B 1234 |
| Chain | Residue |
| B | ILE79 |
| B | ILE86 |
| B | ASN88 |
| B | ILE90 |
| B | ASP105 |
| B | MET107 |
| B | ILE115 |
| B | VAL117 |
| B | GLN121 |
| B | TYR141 |
| B | ARG142 |
| B | PHE143 |
| B | PHE144 |
| B | PHE150 |
| B | TYR158 |
| B | MET202 |
| B | ASN206 |
| B | PRO207 |
| B | VAL208 |
| B | TYR211 |
| B | PHE230 |
| B | HOH2209 |
| B | HOH2210 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18662988","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21050180","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VCK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor for A-ring reduction","evidences":[{"source":"PubMed","id":"21050180","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18662988","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2VCK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18662988","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21050180","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X9J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18662988","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21050180","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X9J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18662988","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21050180","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X9J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21050180","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X9I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 306 |
| Chain | Residue | Details |
| A | ASP105 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
| A | ASN206 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 306 |
| Chain | Residue | Details |
| B | ASP105 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
| B | ASN206 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
