Research workbench
X-ray crystal structure of tmpa, 2-trimethylaminoethylphosphonate hydroxylase, with fe, 2OG, and 2-trimethylaminoethylphosphonate
Analyse X-ray crystal structure of tmpa, 2-trimethylaminoethylphosphonate hydroxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NPC
- Type
- protein
- Length
- 750 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- AKG, KVV, FE2, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 378 | — | — |
| B | — | protein | 372 | — | — |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- KVV · N,N,N-trimethyl-2-phosphonoethan-1-aminium · ligand · chains A
- FE2 · Fe (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NPC · X-ray crystal structure of TmpA, 2-trimethylaminoethylphosphonate hydroxylase, with Fe… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6NPC · PDBe 6NPC
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