6NPC
X-ray crystal structure of TmpA, 2-trimethylaminoethylphosphonate hydroxylase, with Fe, 2OG, and 2-trimethylaminoethylphosphonate
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 | 4 |
Details | binding site for residue FE2 A 401 |
Chain | Residue |
A | HIS198 |
A | ASP200 |
A | HIS341 |
A | AKG402 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue AKG A 402 |
Chain | Residue |
A | HIS341 |
A | ARG343 |
A | ARG352 |
A | LEU354 |
A | FE2401 |
A | KVV403 |
A | HOH544 |
A | VAL179 |
A | LEU195 |
A | HIS198 |
A | ASP200 |
A | GLN211 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue KVV A 403 |
Chain | Residue |
A | TYR173 |
A | PHE177 |
A | ASN187 |
A | TYR190 |
A | ASP200 |
A | ASN201 |
A | TYR203 |
A | ASN286 |
A | ARG288 |
A | TYR358 |
A | AKG402 |
A | HOH548 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue FE2 B 401 |
Chain | Residue |
B | HIS198 |
B | ASP200 |
B | HIS341 |
B | HOH616 |
B | HOH660 |
B | HOH694 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue SO4 B 402 |
Chain | Residue |
A | HOH605 |
B | ASP200 |
B | ASN201 |
B | TYR203 |
B | ASN286 |
B | ARG288 |
B | HOH660 |
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 |