MolNFT v1 · #46349 · protein
Structure of full length GRP94 with AMP-pnp bound
2O1U · Endoplasmin: “Structure of full length GRP94 with AMP-pnp bound”. X-ray diffraction, 2 ligands (ANP, MG), 20 pockets (best druggability 0.80). MolNFT v1 #46349 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2O1U
- Type
- protein
- Length
- 1,153 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmin
- UniProt
- P41148
- Ligands
- ANP, MG
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoplasmin | protein | 578 | 37% helix, 20% strand | P41148 |
| B | Endoplasmin | protein | 575 | 39% helix, 21% strand | P41148 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 788 | 0.80 | 0.83 | 90 | empty |
| 2 | 296 | 0.60 | 0.79 | 38 | empty |
| 3 | 311 | 0.60 | 0.78 | 35 | empty |
| 4 | 125 | 0.51 | 0.80 | 16 | ANP |
| 5 | 144 | 0.50 | 0.79 | 19 | ANP |
Interfaces
1 interface between chains.
- A–B · 1778 Ų buried · 14 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 2O1U · PDBe 2O1U · UniProt P41148
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