MolNFT v1 · #116081 · protein
Directed evolutionary changes in kemp eliminase KE07 - crystal 3 wild type
5D2T · De novo designed kemp eliminase KE07: “Directed evolutionary changes in kemp eliminase KE07 - crystal 3 wild type”. X-ray diffraction, 1 ligand (6VP), 1 pocket (best druggability 0.62). MolNFT v1 #116081 on GenesisL1: 3D structure…
- PDB
- 5D2T
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- De novo designed kemp eliminase KE07
- EC
- 4.1.3.-
- Ligands
- 6VP
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | De novo designed kemp eliminase KE07 (EC 4.1.3.-) | protein | 251 | 40% helix, 25% strand | — |
Ligands and binding sites
- 6VP · 5-nitro-2-oxidanyl-benzenecarbonitrile · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.62 | 0.80 | 38 | 6VP |
Compared structures
- 5D2T · Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 3 Wild Type · 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 5D2T · PDBe 5D2T
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