Research workbench
Structure of P97 N-D1 R155H mutant in complex with atpgs
Analyse Structure of P97 N-D1 R155H mutant in complex with atpgs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HU3
- Type
- protein
- Length
- 899 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transitional endoplasmic reticulum ATPase
- UniProt
- P55072
- Ligands
- AGS, MG
- Pockets
- 10 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transitional endoplasmic reticulum ATPase | protein | 453 | 39% helix, 22% strand | P55072 |
| B | Transitional endoplasmic reticulum ATPase | protein | 446 | 37% helix, 22% strand | P55072 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1059 | 0.85 | 0.86 | 112 | AGS, MG |
| 2 | 442 | 0.70 | 0.81 | 41 | empty |
| 3 | 542 | 0.64 | 0.76 | 34 | empty |
| 4 | 57 | 0.61 | 0.92 | 15 | empty |
| 5 | 152 | 0.58 | 0.83 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 2026 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 3HU3 · Structure of p97 N-D1 R155H mutant in complex with ATPgS · 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 3HU3 · PDBe 3HU3 · UniProt P55072
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