MolNFT v1 · #116091 · protein
Directed evolutionary changes in kemp eliminase KE07 - crystal 17 round 7-2
5D38 · De novo kemp eliminase KE07 round 7-2: “Directed evolutionary changes in kemp eliminase KE07 - crystal 17 round 7-2”. X-ray diffraction, 4 pockets (best druggability 0.65). MolNFT v1 #116091 on GenesisL1: 3D structure, binding sites…
- PDB
- 5D38
- Type
- protein
- Length
- 526 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- De novo kemp eliminase KE07 round 7-2
- EC
- 4.1.3.-
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | De novo kemp eliminase KE07 round 7-2 (EC 4.1.3.-) | protein | 263 | 38% helix, 24% strand | — |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.65 | 0.80 | 49 | empty |
| 2 | 356 | 0.62 | 0.78 | 46 | empty |
| 3 | 272 | 0.50 | 0.74 | 40 | empty |
| 4 | 71 | 0.33 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 509 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5D38 · Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 17 round 7-2 · 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
- Elsewhere: RCSB PDB 5D38 · PDBe 5D38
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