Research workbench
Directed evolutionary changes in kemp eliminase KE07 - crystal 21 round 5
Analyse Directed evolutionary changes in kemp eliminase KE07 - crystal 21 round 5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DKV
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kemp eliminase KE07
- Ligands
- 6VP
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kemp eliminase KE07 | protein | 250 | 41% helix, 24% strand | — |
Ligands and binding sites
- 6VP · 5-nitro-2-oxidanyl-benzenecarbonitrile · ligand · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.59 | 0.82 | 31 | PEG, 6VP |
| 2 | 102 | 0.46 | 0.80 | 24 | empty |
Compared structures
- 6DKV · Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 21 round 5 · 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 6DKV · PDBe 6DKV
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