Research workbench
Structure of middle plus C-terminal domains (M+C) of GRP94
Analyse Structure of middle plus C-terminal domains (M+C) of GRP94 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O1T
- Type
- protein
- Length
- 4,130 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmin
- UniProt
- P41148
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Endoplasmin | protein | 413 | 44% helix, 17% strand | P41148 |
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 | 1115 | 0.80 | 0.81 | 109 | empty |
| 2 | 1138 | 0.80 | 0.81 | 108 | empty |
| 3 | 1017 | 0.79 | 0.81 | 89 | empty |
| 4 | 1124 | 0.79 | 0.81 | 94 | empty |
| 5 | 813 | 0.79 | 0.82 | 77 | empty |
Interfaces
16 interfaces between chains.
- F–G · 2408 Ų buried · 22 hydrogen bonds · protein-protein
- D–E · 2337 Ų buried · 13 hydrogen bonds · protein-protein
- A–J · 2310 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 2220 Ų buried · 12 hydrogen bonds · protein-protein
- H–I · 2215 Ų buried · 16 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 2O1T · PDBe 2O1T · UniProt P41148
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