Research workbench
P47-bound P97-R155H mutant with atpgammas
Analyse P47-bound P97-R155H mutant with atpgammas in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R7S
- Type
- protein
- Length
- 4,207 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transitional endoplasmic reticulum ATPase; NSFL1 cofactor P47
- EC
- 3.6.4.6
- UniProt
- P55072, O35987
- Ligands
- AGS
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 8 distinct chains · 36% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 722 | 32% helix, 12% strand | P55072 |
| B | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 551 | 41% helix, 9% strand | P55072 |
| C | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 546 | 41% helix, 9% strand | P55072 |
| D | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 721 | 37% helix, 15% strand | P55072 |
| E | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 717 | 36% helix, 15% strand | P55072 |
| F | Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) | protein | 733 | 33% helix, 12% strand | P55072 |
| I | NSFL1 cofactor P47 | protein | 113 | 25% helix, 13% strand | O35987 |
| J | NSFL1 cofactor P47 | protein | 104 | 28% helix, 17% strand | O35987 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · 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 | 767 | 0.84 | 0.87 | 98 | AGS |
| 2 | 1195 | 0.83 | 0.85 | 137 | AGS |
| 3 | 1169 | 0.83 | 0.84 | 138 | AGS |
| 4 | 630 | 0.83 | 0.88 | 85 | empty |
| 5 | 587 | 0.82 | 0.87 | 88 | AGS |
Interfaces
13 interfaces between chains.
- A–B · 4174 Ų buried · 40 hydrogen bonds · protein-protein
- D–E · 4117 Ų buried · 47 hydrogen bonds · protein-protein
- E–F · 4026 Ų buried · 41 hydrogen bonds · protein-protein
- A–F · 3987 Ų buried · 41 hydrogen bonds · protein-protein
- C–D · 3964 Ų buried · 40 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 P55072
- Every structure of UniProt O35987
- Elsewhere: RCSB PDB 7R7S · PDBe 7R7S · UniProt P55072 · UniProt O35987
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