MolNFT v2 · #16938 · protein
Crystal Analysis Of Chorismate Mutase From Thermus Thermophilus.
1ODE: “Crystal Analysis Of Chorismate Mutase From Thermus Thermophilus.”. X-ray diffraction at 1.65. MolNFT v2 #16938 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ODE
- Type
- protein
- Length
- 346 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.65
- Source
- THERMUS THERMOPHILUS
Structure
x-ray diffraction · resolution 1.65 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 116 | — | — |
| B, C | — | protein | 115 | — | — |
Compared structures
- 1ODE · Crystal analysis of chorismate mutase from thermus thermophilus. · 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 1ODE · PDBe 1ODE
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