MolNFT v1 · #25047 · protein
Crystal structure of PH0226 protein from pyrococcus horikoshii OT3
1VE3 · Hypothetical protein PH0226: “Crystal structure of PH0226 protein from pyrococcus horikoshii OT3”. X-ray diffraction, 1 ligand (SAM), 3 pockets (best druggability 0.68). MolNFT v1 #25047 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1VE3
- Type
- protein
- Length
- 438 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein PH0226
- UniProt
- O57965
- Ligands
- SAM
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein PH0226 | protein | 212 | 35% helix, 31% strand | O57965 |
| B | Hypothetical protein PH0226 | protein | 226 | 40% helix, 33% strand | O57965 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 251 | 0.68 | 0.84 | 40 | SAM |
| 2 | 193 | 0.63 | 0.84 | 34 | SAM |
| 3 | 343 | 0.61 | 0.77 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 17 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 1VE3 · Crystal structure of PH0226 protein 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 O57965
- Elsewhere: RCSB PDB 1VE3 · PDBe 1VE3 · UniProt O57965
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