MolNFT v1 · #25337 · protein
Crystal structure of vitelline membrane outer layer protein I (vmo-I): a folding motif with homologous greek key structures related by an internal three-fold symmetry
1VMO: “Crystal structure of vitelline membrane outer layer protein I (vmo-I): a folding motif with homologous greek…”. X-ray diffraction, 7 pockets (best druggability 0.58). MolNFT v1 #25337 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1VMO
- Type
- protein
- Length
- 326 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vitelline membrane outer layer protein I
- UniProt
- P41366
- Pockets
- 7 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Vitelline membrane outer layer protein I | protein | 163 | 0% helix, 39% strand | P41366 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.58 | 0.81 | 27 | empty |
| 2 | 110 | 0.46 | 0.79 | 20 | empty |
| 3 | 114 | 0.43 | 0.78 | 18 | empty |
| 4 | 115 | 0.40 | 0.76 | 20 | empty |
| 5 | 53 | 0.34 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 388 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1VMO · Crystal structure of vitelline membrane outer layer protein I (vmo-I): a folding motif… · the same entry in another collection · chain A against A, TM-score 1.00
- P41366 · AlphaFold monomer V2.0 prediction for vitelline membrane outer layer protein 1 (P41366) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P41366
- Elsewhere: RCSB PDB 1VMO · PDBe 1VMO · UniProt P41366
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