4TME
Crystal Structure of EutL from Clostridium Perfringens bound to ethanolamine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005198 | molecular_function | structural molecule activity |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0031469 | cellular_component | bacterial microcompartment |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005198 | molecular_function | structural molecule activity |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0031469 | cellular_component | bacterial microcompartment |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005198 | molecular_function | structural molecule activity |
| C | 0031419 | molecular_function | cobalamin binding |
| C | 0031469 | cellular_component | bacterial microcompartment |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 301 |
| Chain | Residue |
| A | ASN74 |
| A | HOH497 |
| B | ASN74 |
| B | HOH510 |
| C | ASN74 |
| C | HOH479 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ETA A 302 |
| Chain | Residue |
| A | PHE184 |
| A | HOH437 |
| A | HOH447 |
| A | ASP45 |
| A | PHE176 |
| A | THR180 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue ETA A 303 |
| Chain | Residue |
| A | CYS43 |
| A | ASP44 |
| A | GLU82 |
| A | PHE112 |
| A | THR182 |
| A | PHE184 |
| A | HOH437 |
| A | HOH444 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 301 |
| Chain | Residue |
| B | LEU165 |
| B | ALA168 |
| B | HOH432 |
| B | HOH433 |
| B | HOH529 |
| B | HOH573 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue ETA B 302 |
| Chain | Residue |
| B | ASP45 |
| B | PHE176 |
| B | THR180 |
| B | PHE184 |
| B | HOH452 |
| B | HOH459 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue ETA B 303 |
| Chain | Residue |
| B | CYS43 |
| B | ASP44 |
| B | GLU82 |
| B | PHE112 |
| B | THR182 |
| B | PHE184 |
| B | HOH467 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue ETA C 301 |
| Chain | Residue |
| C | ASP45 |
| C | PHE176 |
| C | THR180 |
| C | PHE184 |
| C | HOH440 |
| C | HOH445 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue ETA C 302 |
| Chain | Residue |
| C | CYS43 |
| C | ASP44 |
| C | GLU82 |
| C | PHE112 |
| C | THR182 |
| C | PHE184 |
| C | HOH443 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 327 |
| Details | Domain: {"description":"BMC circularly permuted 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01279","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 318 |
| Details | Domain: {"description":"BMC circularly permuted 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01279","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"25484204","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4U6I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25752492","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TME","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4TME","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | Site: {"description":"Important for gating","evidences":[{"source":"PubMed","id":"25752492","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
