MolNFT v1 · #34176 · protein
Crystal structure of PH0655 from pyrococcus horikoshii OT3
2D8A · Probable L-threonine 3-dehydrogenase: “Crystal structure of PH0655 from pyrococcus horikoshii OT3”. X-ray diffraction, 2 ligands (NAD, ZN), 1 pocket (best druggability 0.65). MolNFT v1 #34176 on GenesisL1: 3D structure, binding…
- PDB
- 2D8A
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable L-threonine 3-dehydrogenase
- EC
- 1.1.1.103
- UniProt
- O58389
- Ligands
- NAD, ZN
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable L-threonine 3-dehydrogenase (EC 1.1.1.103) | protein | 333 | 29% helix, 28% strand | O58389 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- ZN · Zinc ion · metal · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 507 | 0.65 | 0.77 | 52 | ZN, NAD |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O58389
- Elsewhere: RCSB PDB 2D8A · PDBe 2D8A · UniProt O58389
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