Research workbench
N-domain of GRP94 lacking the charged domain in complex with radicicol
Analyse N-domain of GRP94 lacking the charged domain in complex with radicicol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U0Z
- Type
- protein
- Length
- 437 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmin
- UniProt
- P41148
- Ligands
- RDC
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoplasmin | protein | 211 | 41% helix, 25% strand | P41148 |
| B | Endoplasmin | protein | 226 | 42% helix, 24% strand | P41148 |
Ligands and binding sites
- RDC · Radicicol · ligand · 2 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · 9 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 | 273 | 0.63 | 0.80 | 30 | RDC |
| 2 | 260 | 0.60 | 0.79 | 27 | RDC |
| 3 | 362 | 0.59 | 0.76 | 36 | 1PE |
| 4 | 95 | 0.34 | 0.73 | 24 | PG4 |
| 5 | 80 | 0.31 | 0.74 | 20 | PG4 |
Interfaces
1 interface between chains.
- A–B · 452 Ų buried · 12 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 1U0Z · PDBe 1U0Z · UniProt P41148
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