Research workbench
Crystal structure of ralstonia sp. alcohol dehydrogenase mutant N15G, G37D, R38V, R39S, A86N, S88A
Analyse Crystal structure of ralstonia sp. alcohol dehydrogenase mutant N15G, G37D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I5G
- Type
- protein
- Length
- 1,864 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alclohol DEHYDROGENASE/SHORT-chain dehydrogenase
- UniProt
- C0IR58
- Pockets
- 17 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Alclohol DEHYDROGENASE/SHORT-chain dehydrogenase | protein | 233 | 45% helix, 20% strand | C0IR58 |
Pockets
17 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1086 | 0.84 | 0.85 | 81 | empty |
| 2 | 1074 | 0.84 | 0.85 | 79 | empty |
| 3 | 617 | 0.67 | 0.77 | 44 | empty |
| 4 | 576 | 0.67 | 0.77 | 40 | empty |
| 5 | 320 | 0.62 | 0.79 | 40 | empty |
Interfaces
15 interfaces between chains.
- A–B · 1609 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 1608 Ų buried · 27 hydrogen bonds · protein-protein
- E–F · 1606 Ų buried · 26 hydrogen bonds · protein-protein
- G–H · 1596 Ų buried · 30 hydrogen bonds · protein-protein
- A–C · 1559 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 4I5G · Crystal structure of Ralstonia sp. alcohol dehydrogenase mutant N15G, G37D, R38V, R39S… · the same entry in another collection · chain A against A, TM-score 1.00
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 C0IR58
- Elsewhere: RCSB PDB 4I5G · PDBe 4I5G · UniProt C0IR58
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