1X1A
Crystal structure of BchU complexed with S-adenosyl-L-methionine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0015995 | biological_process | chlorophyll biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030494 | biological_process | bacteriochlorophyll biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 0036069 | biological_process | light-dependent bacteriochlorophyll biosynthetic process |
| A | 0036070 | biological_process | light-independent bacteriochlorophyll biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 4396 |
| Chain | Residue |
| A | ASN74 |
| A | GLU84 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAM A 4264 |
| Chain | Residue |
| A | ASP227 |
| A | ILE228 |
| A | TYR229 |
| A | CYS242 |
| A | ARG243 |
| A | HOH4452 |
| A | HOH4460 |
| A | GLU147 |
| A | HIS150 |
| A | GLY177 |
| A | GLY179 |
| A | ASN200 |
| A | LEU201 |
| A | VAL226 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 2431 |
| Chain | Residue |
| A | ARG140 |
| A | HOH4461 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"16797589","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16797589","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1X1A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X1B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X1C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X1D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16797589","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16797589","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1kyw |
| Chain | Residue | Details |
| A | TYR246 |
