MolNFT v1 · #174240 · protein
Human aaa+ ATPase vcp mutant - T76E, ADP-bound form
7BP9 · Transitional endoplasmic reticulum ATPase: “Human aaa+ ATPase vcp mutant - T76E, ADP-bound form”. Electron microscopy, 1 ligand (ADP), 20 pockets (best druggability 0.82). MolNFT v1 #174240 on GenesisL1: 3D structure, binding sites…
- PDB
- 7BP9
- Type
- protein
- Length
- 4,440 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transitional endoplasmic reticulum ATPase
- EC
- 3.6.4.6
- UniProt
- P55072
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 740 | 39% helix, 17% strand | P55072 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 12 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 911 | 0.82 | 0.84 | 104 | ADP |
| 2 | 1172 | 0.81 | 0.82 | 132 | ADP |
| 3 | 440 | 0.80 | 0.88 | 65 | empty |
| 4 | 396 | 0.80 | 0.88 | 62 | empty |
| 5 | 772 | 0.78 | 0.82 | 76 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3349 Ų buried · 25 hydrogen bonds · protein-protein
- D–E · 3327 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 3319 Ų buried · 25 hydrogen bonds · protein-protein
- E–F · 3302 Ų buried · 25 hydrogen bonds · protein-protein
- A–F · 3276 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 7BP9 · Human AAA+ ATPase VCP mutant - T76E, ADP-bound form · 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 P55072
- Elsewhere: RCSB PDB 7BP9 · PDBe 7BP9 · UniProt P55072
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