6NPB
X-ray crystal structure of TmpA, 2-trimethylaminoethylphosphonate hydroxylase, with Fe and 2OG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0008336 | molecular_function | gamma-butyrobetaine dioxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0045329 | biological_process | carnitine biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0008336 | molecular_function | gamma-butyrobetaine dioxygenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| B | 0045329 | biological_process | carnitine biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 A 401 |
| Chain | Residue |
| A | HIS198 |
| A | ASP200 |
| A | HIS341 |
| A | AKG402 |
| A | HOH527 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue AKG A 402 |
| Chain | Residue |
| A | ASP200 |
| A | GLN211 |
| A | HIS341 |
| A | ARG343 |
| A | ARG352 |
| A | LEU354 |
| A | FE2401 |
| A | HOH508 |
| A | HOH527 |
| A | PHE177 |
| A | VAL179 |
| A | LEU195 |
| A | HIS198 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ASN187 |
| A | HIS198 |
| A | ASP200 |
| A | ASN201 |
| A | TYR203 |
| A | ASN286 |
| A | ARG288 |
| A | HOH515 |
| A | HOH527 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | LEU193 |
| A | GLY194 |
| A | GLY345 |
| A | HOH598 |
| A | HOH673 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue FE2 B 401 |
| Chain | Residue |
| B | HIS198 |
| B | ASP200 |
| B | HIS341 |
| B | HOH535 |
| B | HOH621 |
| B | HOH692 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | ASP200 |
| B | ASN201 |
| B | TYR203 |
| B | ASN286 |
| B | ARG288 |
| B | HOH621 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| A | ASP108 |
| A | HOH505 |
| A | HOH607 |
| B | ARG254 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30789718","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NPC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NPD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30789718","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NPC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NPD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30789718","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NPC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
