MolNFT v1 · #39460 · protein
Crystal structure of hypothetical protein PH0414 from pyrococcus horikoshii OT3
2HUN · 336AA long hypothetical dtdp-glucose 4,6-dehydratase: “Crystal structure of hypothetical protein PH0414 from pyrococcus horikoshii OT3”. X-ray diffraction, 1 ligand (NAD), 5 pockets (best druggability 0.86). MolNFT v1 #39460 on…
- PDB
- 2HUN
- Type
- protein
- Length
- 654 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 336AA long hypothetical dtdp-glucose 4,6-dehydratase
- EC
- 4.2.1.46
- UniProt
- O58151
- Ligands
- NAD
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 336AA long hypothetical dtdp-glucose 4,6-dehydratase (EC 4.2.1.46) | protein | 329 | 43% helix, 18% strand | O58151 |
| B | 336AA long hypothetical dtdp-glucose 4,6-dehydratase (EC 4.2.1.46) | protein | 325 | 43% helix, 19% strand | O58151 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 722 | 0.86 | 0.89 | 70 | NAD |
| 2 | 999 | 0.81 | 0.83 | 80 | NAD |
| 3 | 108 | 0.41 | 0.76 | 16 | empty |
| 4 | 82 | 0.37 | 0.76 | 14 | empty |
| 5 | 68 | 0.35 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1330 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2HUN · Crystal structure of hypothetical protein PH0414 from Pyrococcus horikoshii OT3 · 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
- Every structure of UniProt O58151
- Elsewhere: RCSB PDB 2HUN · PDBe 2HUN · UniProt O58151
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