MolNFT v1 · #16945 · protein
Cephalosporin C deacetylase mutated, in complex with acetate
1ODT: “Cephalosporin C deacetylase mutated, in complex with acetate”. X-ray diffraction, 3 pockets (best druggability 0.55). MolNFT v1 #16945 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ODT
- Type
- protein
- Length
- 634 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cephalosporin C deacetylase
- EC
- 3.1.1.41
- UniProt
- P94388
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, H | Cephalosporin C deacetylase (EC 3.1.1.41) | protein | 317 | 38% helix, 21% strand | P94388 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains C, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.55 | 0.77 | 34 | ACT |
| 2 | 186 | 0.52 | 0.77 | 24 | empty |
| 3 | 80 | 0.34 | 0.75 | 21 | ACT |
Interfaces
1 interface between chains.
- C–H · 1248 Ų buried · 35 hydrogen bonds · protein-protein
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 P94388
- Elsewhere: RCSB PDB 1ODT · PDBe 1ODT · UniProt P94388
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