Research workbench
Crystal structure of cephalosporin acylase from bacillus halodurans
Analyse Crystal structure of cephalosporin acylase from bacillus halodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NLZ
- Type
- protein
- Length
- 2,143 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cephalosporin acylase
- UniProt
- Q9KEI5
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cephalosporin acylase | protein | 536 | 37% helix, 19% strand | Q9KEI5 |
| B, C | Cephalosporin acylase | protein | 535 | 36% helix, 19% strand | Q9KEI5 |
| D | Cephalosporin acylase | protein | 537 | 36% helix, 19% strand | Q9KEI5 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.82 | 0.96 | 56 | empty |
| 2 | 196 | 0.82 | 0.95 | 51 | empty |
| 3 | 673 | 0.77 | 0.82 | 71 | empty |
| 4 | 251 | 0.72 | 0.87 | 27 | empty |
| 5 | 245 | 0.71 | 0.86 | 23 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2854 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 2802 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 765 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 760 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 203 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2NLZ · Crystal structure of cephalosporin acylase from Bacillus halodurans · the same entry in another collection · chain B against B, 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
- Every structure of UniProt Q9KEI5
- Elsewhere: RCSB PDB 2NLZ · PDBe 2NLZ · UniProt Q9KEI5
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