Research workbench
Crystal structure of the P21 R1-R7 N-terminal domain of murine mvp
Analyse Crystal structure of the P21 R1-R7 N-terminal domain of murine mvp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GF5
- Type
- protein
- Length
- 758 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major vault protein
- UniProt
- Q9EQK5
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major vault protein | protein | 378 | 0% helix, 49% strand | Q9EQK5 |
| B | Major vault protein | protein | 380 | 0% helix, 49% strand | Q9EQK5 |
Ligands and binding sites
- GOL · Glycerol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 786 | 0.74 | 0.79 | 60 | empty |
| 2 | 419 | 0.64 | 0.78 | 44 | GOL |
| 3 | 85 | 0.39 | 0.77 | 16 | empty |
| 4 | 122 | 0.37 | 0.73 | 20 | empty |
| 5 | 65 | 0.34 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1028 Ų buried · 16 hydrogen bonds · protein-protein
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 Q9EQK5
- Elsewhere: RCSB PDB 3GF5 · PDBe 3GF5 · UniProt Q9EQK5
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