3NEV
Crystal structure of YagE, a prophage protein from E. coli K12 in complex with KDGal
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046176 | biological_process | aldonic acid catabolic process |
| A | 0047440 | molecular_function | 2-dehydro-3-deoxy-D-pentonate aldolase activity |
| A | 0061677 | molecular_function | 2-dehydro-3-deoxy-D-gluconate aldolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046176 | biological_process | aldonic acid catabolic process |
| B | 0047440 | molecular_function | 2-dehydro-3-deoxy-D-pentonate aldolase activity |
| B | 0061677 | molecular_function | 2-dehydro-3-deoxy-D-gluconate aldolase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0016829 | molecular_function | lyase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046176 | biological_process | aldonic acid catabolic process |
| C | 0047440 | molecular_function | 2-dehydro-3-deoxy-D-pentonate aldolase activity |
| C | 0061677 | molecular_function | 2-dehydro-3-deoxy-D-gluconate aldolase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0016829 | molecular_function | lyase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046176 | biological_process | aldonic acid catabolic process |
| D | 0047440 | molecular_function | 2-dehydro-3-deoxy-D-pentonate aldolase activity |
| D | 0061677 | molecular_function | 2-dehydro-3-deoxy-D-gluconate aldolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 2 |
| Chain | Residue |
| A | LEU54 |
| A | TYR145 |
| A | PHE60 |
| A | ARG68 |
| A | GLY88 |
| A | THR89 |
| A | GLY90 |
| A | VAL113 |
| A | VAL114 |
| A | ILE115 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 5 |
| Chain | Residue |
| A | ASN126 |
| A | ARG129 |
| A | HOH339 |
| A | HOH449 |
| B | SER289 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE RSH A 1 |
| Chain | Residue |
| A | PRO20 |
| A | PHE52 |
| A | GLY55 |
| A | SER56 |
| A | GLY57 |
| A | TYR145 |
| A | PHE147 |
| A | LYS174 |
| A | THR176 |
| A | GLY202 |
| A | ILE219 |
| A | SER220 |
| A | ALA221 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 3 |
| Chain | Residue |
| B | LEU54 |
| B | GLY55 |
| B | PHE60 |
| B | GLY88 |
| B | GLY90 |
| B | VAL113 |
| B | VAL114 |
| B | ILE115 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 4 |
| Chain | Residue |
| A | PRO286 |
| A | PRO287 |
| A | ALA288 |
| B | ASN126 |
| B | ARG129 |
| B | TYR130 |
| B | GLN133 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RSH B 2 |
| Chain | Residue |
| B | PRO20 |
| B | PHE52 |
| B | GLY55 |
| B | SER56 |
| B | GLY57 |
| B | TYR145 |
| B | LYS174 |
| B | THR176 |
| B | GLY202 |
| B | ILE219 |
| B | SER220 |
| B | ALA221 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO C 1 |
| Chain | Residue |
| C | LEU54 |
| C | PHE60 |
| C | ARG68 |
| C | GLY88 |
| C | THR89 |
| C | GLY90 |
| C | VAL113 |
| C | VAL114 |
| C | ILE115 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 7 |
| Chain | Residue |
| C | HIS283 |
| C | VAL284 |
| C | ALA288 |
| C | PRO290 |
| C | HOH372 |
| D | ARG129 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE RSH C 3 |
| Chain | Residue |
| C | PRO20 |
| C | PHE52 |
| C | GLY55 |
| C | SER56 |
| C | GLY57 |
| C | TYR145 |
| C | LYS174 |
| C | THR176 |
| C | GLY202 |
| C | TYR203 |
| C | ILE219 |
| C | SER220 |
| C | ALA221 |
| C | HOH392 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 6 |
| Chain | Residue |
| D | LEU54 |
| D | GLY55 |
| D | PHE60 |
| D | GLY88 |
| D | GLY90 |
| D | VAL113 |
| D | VAL114 |
| D | ILE115 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO D 8 |
| Chain | Residue |
| D | HOH332 |
| D | HOH337 |
| D | HOH366 |
| D | HOH456 |
| C | ALA125 |
| C | ARG129 |
| C | HOH454 |
| D | ASP262 |
| D | ASP292 |
| D | ARG295 |
| D | HOH313 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE RSH D 4 |
| Chain | Residue |
| D | PRO20 |
| D | PHE52 |
| D | GLY55 |
| D | SER56 |
| D | GLY57 |
| D | TYR145 |
| D | PHE147 |
| D | LYS174 |
| D | THR176 |
| D | GLY202 |
| D | ILE219 |
| D | SER220 |
| D | ALA221 |
| D | HOH453 |
| D | HOH480 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"21294156","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21294156","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"21294156","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |






