Research workbench
Beta-ketoacyl-acp synthase II from escherichia COLI
Analyse Beta-ketoacyl-acp synthase II from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KAS
- Type
- protein
- Length
- 411 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-ketoacyl acp synthase II
- EC
- 2.3.1.41
- UniProt
- P0AAI5
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-ketoacyl acp synthase II (EC 2.3.1.41) | protein | 411 | 38% helix, 21% strand | P0AAI5 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.67 | 0.87 | 35 | empty |
| 2 | 72 | 0.38 | 0.78 | 15 | empty |
| 3 | 52 | 0.24 | 0.72 | 13 | 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 P0AAI5
- Elsewhere: RCSB PDB 1KAS · PDBe 1KAS · UniProt P0AAI5
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