MolNFT v1 · #28925 · protein
Crystal structure of the unliganded form of GRP94, the er HSP90: basis for nucleotide-induced conformational change, GRP94N(DELTA)41 apo crystal
1YT1 · Endoplasmin: “Crystal structure of the unliganded form of GRP94, the er HSP90: basis for nucleotide-induced conformational…”. X-ray diffraction, 5 pockets (best druggability 0.62). MolNFT v1 #28925 on GenesisL1: 3D structure…
- PDB
- 1YT1
- Type
- protein
- Length
- 459 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmin
- UniProt
- P41148
- Pockets
- 5 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoplasmin | protein | 227 | 40% helix, 24% strand | P41148 |
| B | Endoplasmin | protein | 232 | 44% helix, 23% strand | P41148 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 11 copies · chains A, B
- 1PE · Pentaethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.62 | 0.81 | 24 | PG4 |
| 2 | 218 | 0.62 | 0.81 | 28 | PG4 |
| 3 | 387 | 0.60 | 0.76 | 33 | 1PE |
| 4 | 84 | 0.32 | 0.74 | 20 | PG4 |
| 5 | 66 | 0.29 | 0.73 | 18 | PG4 |
Interfaces
1 interface between chains.
- A–B · 452 Ų buried · 13 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 P41148
- Elsewhere: RCSB PDB 1YT1 · PDBe 1YT1 · UniProt P41148
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.