2W8S
CRYSTAL STRUCTURE OF A catalytically promiscuous PHOSPHONATE MONOESTER HYDROLASE FROM Burkholderia caryophylli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008484 | molecular_function | sulfuric ester hydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008484 | molecular_function | sulfuric ester hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008484 | molecular_function | sulfuric ester hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008484 | molecular_function | sulfuric ester hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1515 |
| Chain | Residue |
| A | ASP12 |
| A | FGL57 |
| A | ASP324 |
| A | HIS325 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A1516 |
| Chain | Residue |
| A | ASP12 |
| A | FGL57 |
| A | ASP324 |
| A | HIS325 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1515 |
| Chain | Residue |
| B | FGL57 |
| B | ASP324 |
| B | HIS325 |
| B | ASP12 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE B1516 |
| Chain | Residue |
| B | ASP12 |
| B | FGL57 |
| B | ASP324 |
| B | HIS325 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C1515 |
| Chain | Residue |
| C | ASP12 |
| C | FGL57 |
| C | ASP324 |
| C | HIS325 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C1516 |
| Chain | Residue |
| C | ASP12 |
| C | FGL57 |
| C | ASP324 |
| C | HIS325 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D1515 |
| Chain | Residue |
| D | ASP12 |
| D | FGL57 |
| D | ASP324 |
| D | HIS325 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D1516 |
| Chain | Residue |
| D | ASP12 |
| D | FGL57 |
| D | ASP324 |
| D | HIS325 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B1517 |
| Chain | Residue |
| B | ARG392 |
| B | ARG407 |
| B | HIS494 |
| B | HOH2202 |
| B | HOH2203 |
| B | HOH2204 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C1517 |
| Chain | Residue |
| C | ARG392 |
| C | HIS494 |
| C | HOH2247 |
| C | HOH2248 |
| C | HOH2249 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D1517 |
| Chain | Residue |
| D | ARG392 |
| D | HIS494 |
| D | HOH2202 |
| D | HOH2203 |
| D | HOH2204 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A1517 |
| Chain | Residue |
| A | ARG392 |
| A | ARG407 |
| A | HIS494 |
| A | HOH2156 |
| A | HOH2157 |
| A | HOH2158 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D1518 |
| Chain | Residue |
| D | ARG263 |
| D | GLU272 |
| D | GLY273 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C1518 |
| Chain | Residue |
| C | ARG263 |
| C | GLU272 |
| C | GLY273 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C1519 |
| Chain | Residue |
| A | GLN151 |
| C | LEU197 |
| C | LYS201 |
| C | ARG303 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D1519 |
| Chain | Residue |
| B | GLN151 |
| D | LEU197 |
| D | LYS201 |
| D | ARG303 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D1520 |
| Chain | Residue |
| D | ARG263 |
| D | GLY273 |
| D | SER274 |
| D | THR277 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D1521 |
| Chain | Residue |
| B | SER134 |
| B | GLY136 |
| B | ALA137 |
| B | ARG195 |
| D | SER134 |
| D | GLY136 |
| D | ALA137 |
| D | ARG195 |
| D | HOH2205 |
| D | HOH2206 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D1522 |
| Chain | Residue |
| D | LEU82 |
| D | GLN84 |
| D | ASN88 |
| D | THR108 |
| D | MET129 |
| D | ASP130 |
| D | HOH2207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20133613","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20133613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W8S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"via 3-oxoalanine","evidences":[{"source":"PubMed","id":"20133613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W8S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"3-oxoalanine (Cys)","evidences":[{"source":"PIRSR","id":"PIRSR600917-51","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20133613","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
