MolNFT v1 · #25169 · protein
Crystal structure of an hypothetical protein
1VHM · Protein yebr: “Crystal structure of an hypothetical protein”. X-ray diffraction, 2 pockets (best druggability 0.69). MolNFT v1 #25169 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1VHM
- Type
- protein
- Length
- 319 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein yebr
- UniProt
- P76270
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein yebr | protein | 159 | 39% helix, 26% strand | P76270 |
| B | Protein yebr | protein | 160 | 41% helix, 26% strand | P76270 |
Ligands and binding sites
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.69 | 0.89 | 25 | MES |
| 2 | 115 | 0.65 | 0.89 | 27 | MES |
Interfaces
1 interface between chains.
- A–B · 1202 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P76270
- Elsewhere: RCSB PDB 1VHM · PDBe 1VHM · UniProt P76270
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