Research workbench
Crystal structure of the apo form of mouse mu-crystallin.
Analyse Crystal structure of the apo form of mouse mu-crystallin. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BV8
- Type
- protein
- Length
- 603 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thiomorpholine-carboxylate dehydrogenase
- EC
- 1.5.1.25
- UniProt
- O54983
- Ligands
- K
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiomorpholine-carboxylate dehydrogenase (EC 1.5.1.25) | protein | 303 | 39% helix, 25% strand | O54983 |
| B | Thiomorpholine-carboxylate dehydrogenase (EC 1.5.1.25) | protein | 300 | 39% helix, 25% strand | O54983 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 755 | 0.74 | 0.79 | 64 | empty |
| 2 | 516 | 0.70 | 0.79 | 54 | empty |
| 3 | 396 | 0.63 | 0.78 | 44 | empty |
| 4 | 84 | 0.44 | 0.80 | 15 | empty |
| 5 | 81 | 0.41 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 418 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4BV8 · Crystal structure of the apo form of mouse Mu-crystallin. · the same entry in another collection · chain A against A, TM-score 1.00
- O54983 · AlphaFold monomer V2.0 prediction for ketimine reductase mu- crystallin (O54983) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O54983
- Elsewhere: RCSB PDB 4BV8 · PDBe 4BV8 · UniProt O54983
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