1BVA
MANGANESE BINDING MUTANT IN CYTOCHROME C PEROXIDASE
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 391 |
| Chain | Residue |
| A | GLY41 |
| A | ASP45 |
| A | HIS181 |
| A | HEM390 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM A 390 |
| Chain | Residue |
| A | TRP51 |
| A | PRO145 |
| A | ASP146 |
| A | ALA147 |
| A | LEU171 |
| A | MET172 |
| A | ALA174 |
| A | HIS175 |
| A | GLY178 |
| A | LYS179 |
| A | THR180 |
| A | HIS181 |
| A | ASN184 |
| A | SER185 |
| A | TRP191 |
| A | LEU232 |
| A | THR234 |
| A | PHE262 |
| A | MN391 |
| A | HOH634 |
| A | HOH660 |
| A | HOH776 |
| A | ASP44 |
| A | ASP45 |
| A | VAL47 |
| A | ARG48 |
| site_id | MN |
| Number of Residues | 1 |
| Details | MANGANESE BOUND IN ENGINEERED SITE THE LOOP CONTAINING RESIDUES 33-41 IS REARRANGED. |
| Chain | Residue |
| A | MN391 |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALMGAHAL |
| Chain | Residue | Details |
| A | GLU167-LEU177 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"2851317","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10722697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11170452","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2169873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6092361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8384877","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8673607","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1apx |
| Chain | Residue | Details |
| A | ARG48 | |
| A | HIS52 | |
| A | ASN82 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 709 |
| Chain | Residue | Details |
| A | ARG48 | electrostatic stabiliser |
| A | HIS52 | electrostatic stabiliser, proton acceptor, proton donor |
| A | TRP191 | single electron acceptor, single electron donor |
