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Crystal structure of the rabbit L-gulonate 3-dehydrogenase
Analyse Crystal structure of the rabbit L-gulonate 3-dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ADO
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lambda-crystallin
- EC
- 1.1.1.45
- UniProt
- P14755
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lambda-crystallin (EC 1.1.1.45) | protein | 310 | 55% helix, 13% strand | P14755 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 381 | 0.55 | 0.73 | 35 | empty |
| 2 | 139 | 0.51 | 0.79 | 19 | empty |
| 3 | 60 | 0.35 | 0.77 | 11 | empty |
| 4 | 57 | 0.27 | 0.72 | 11 | empty |
| 5 | 51 | 0.24 | 0.72 | 10 | empty |
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 P14755
- Elsewhere: RCSB PDB 3ADO · PDBe 3ADO · UniProt P14755
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