MolNFT v1 · #186662 · protein
Cryo-EM structure of human P97-D592N mutant bound to ADP.
7RLG · Transitional endoplasmic reticulum ATPase: “Cryo-EM structure of human P97-D592N mutant bound to ADP.”. Electron microscopy, 1 ligand (ADP), 20 pockets (best druggability 0.84). MolNFT v1 #186662 on GenesisL1: 3D structure, binding…
- PDB
- 7RLG
- Type
- protein
- Length
- 4,410 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 0.84
Structure
electron microscopy · 1 distinct chain · 39% helix, 14% 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 | 735 | 39% helix, 14% strand | P55072 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 12 copies · chains A, F, B, C, D, E
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 | 1011 | 0.84 | 0.85 | 124 | ADP |
| 2 | 1180 | 0.84 | 0.85 | 142 | ADP |
| 3 | 1193 | 0.83 | 0.84 | 133 | ADP |
| 4 | 979 | 0.83 | 0.84 | 104 | ADP |
| 5 | 990 | 0.82 | 0.83 | 96 | ADP |
Interfaces
6 interfaces between chains.
- D–E · 4066 Ų buried · 44 hydrogen bonds · protein-protein
- A–F · 4034 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 4025 Ų buried · 46 hydrogen bonds · protein-protein
- E–F · 4011 Ų buried · 44 hydrogen bonds · protein-protein
- C–D · 3962 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 7RLG · Cryo-EM structure of human p97-D592N mutant bound to ADP. · the same entry in another collection · chain C against C, 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 7RLG · PDBe 7RLG · UniProt P55072
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