Research workbench
Structure of human P97 ATPase L464P mutant
Analyse Structure of human P97 ATPase L464P mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MDO
- Type
- protein
- Length
- 3,186 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 0.85
Structure
electron microscopy · 1 distinct chain · 44% helix, 9% 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 | 531 | 44% helix, 9% strand | P55072 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 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 | 723 | 0.85 | 0.89 | 112 | empty |
| 2 | 981 | 0.85 | 0.86 | 116 | ADP |
| 3 | 703 | 0.85 | 0.89 | 108 | empty |
| 4 | 591 | 0.84 | 0.89 | 80 | empty |
| 5 | 568 | 0.84 | 0.89 | 69 | empty |
Interfaces
9 interfaces between chains.
- B–C · 3134 Ų buried · 28 hydrogen bonds · protein-protein
- A–F · 3129 Ų buried · 28 hydrogen bonds · protein-protein
- D–E · 3128 Ų buried · 29 hydrogen bonds · protein-protein
- E–F · 3124 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 3115 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 7MDO · Structure of human p97 ATPase L464P mutant · 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 7MDO · PDBe 7MDO · UniProt P55072
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