3AJG
Crystal structure of PcyA V225D-biliverdin IX alpha complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010024 | biological_process | phytochromobilin biosynthetic process |
| A | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
| A | 0050620 | molecular_function | phycocyanobilin:ferredoxin oxidoreductase activity |
| B | 0010024 | biological_process | phytochromobilin biosynthetic process |
| B | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
| B | 0050620 | molecular_function | phycocyanobilin:ferredoxin oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE BLA A 1131 |
| Chain | Residue |
| A | ILE60 |
| A | THR222 |
| A | ASP225 |
| A | PHE244 |
| B | LYS221 |
| A | LEU84 |
| A | ILE86 |
| A | HIS88 |
| A | ASP105 |
| A | VAL107 |
| A | SER114 |
| A | ALA115 |
| A | GLN216 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BLA B 1130 |
| Chain | Residue |
| B | VAL80 |
| B | LEU84 |
| B | ILE86 |
| B | HIS88 |
| B | ASP105 |
| B | VAL107 |
| B | ILE117 |
| B | ARG149 |
| B | PHE164 |
| B | GLN216 |
| B | ASN219 |
| B | LYS221 |
| B | THR222 |
| B | ASP225 |
| B | LEU226 |
| B | HOH258 |
| B | HOH290 |
| B | HOH319 |
| B | HOH324 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00618","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19887371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16380422","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25872660","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00618","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16380422","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19887371","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25872660","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00618","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16380422","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25872660","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19887371","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2D1E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QCD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16380422","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16380422","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19887371","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00618","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16380422","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25872660","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2D1E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QCD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
