Research workbench
D1 and D2 domain structure of the P97(R155H)-P47 complex
Analyse D1 and D2 domain structure of the P97(R155H)-P47 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R7U
- Type
- protein
- Length
- 3,240 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
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 2 distinct chains · 44% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 538 | 44% helix, 9% strand | P55072 |
| B, D, E, F | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 541 | 44% helix, 9% strand | P55072 |
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 | 784 | 0.85 | 0.88 | 96 | empty |
| 2 | 1105 | 0.85 | 0.86 | 136 | empty |
| 3 | 1013 | 0.85 | 0.86 | 120 | empty |
| 4 | 595 | 0.84 | 0.89 | 93 | empty |
| 5 | 1066 | 0.84 | 0.85 | 120 | empty |
Interfaces
6 interfaces between chains.
- B–C · 3861 Ų buried · 38 hydrogen bonds · protein-protein
- A–F · 3732 Ų buried · 45 hydrogen bonds · protein-protein
- A–B · 3708 Ų buried · 46 hydrogen bonds · protein-protein
- D–E · 3696 Ų buried · 47 hydrogen bonds · protein-protein
- C–D · 3570 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 7R7U · D1 and D2 domain structure of the p97(R155H)-p47 complex · 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 7R7U · PDBe 7R7U · UniProt P55072
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