Research workbench
Cryo-EM structure of human P97 bound to atpgs (conformation I)
Analyse Cryo-EM structure of human P97 bound to atpgs (conformation I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FTL
- Type
- protein
- Length
- 4,338 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 · 41% helix, 15% 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 | 723 | 41% helix, 15% 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 | 1039 | 0.84 | 0.85 | 140 | ADP |
| 2 | 891 | 0.83 | 0.85 | 120 | empty |
| 3 | 850 | 0.83 | 0.85 | 106 | empty |
| 4 | 810 | 0.82 | 0.85 | 106 | empty |
| 5 | 1105 | 0.81 | 0.82 | 113 | empty |
Interfaces
12 interfaces between chains.
- B–C · 2983 Ų buried · 16 hydrogen bonds · protein-protein
- D–E · 2980 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 2979 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 2976 Ų buried · 16 hydrogen bonds · protein-protein
- A–F · 2971 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 5FTL · Cryo-EM structure of human p97 bound to ATPgS (Conformation I) · 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 5FTL · PDBe 5FTL · UniProt P55072
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