Research workbench
Mutations in cephalosporin acylase affecting stability and autoproteolysis
Analyse Mutations in cephalosporin acylase affecting stability and autoproteolysis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JTQ
- Type
- protein
- Length
- 676 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaryl 7-aminocephalosporanic acid acylase
- EC
- 3.5.1.93
- UniProt
- A4ZVL3
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaryl 7-aminocephalosporanic acid acylase (EC 3.5.1.93) | protein | 154 | 68% helix, 6% strand | A4ZVL3 |
| B | Glutaryl 7-aminocephalosporanic acid acylase (EC 3.5.1.93) | protein | 522 | 25% helix, 30% strand | A4ZVL3 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 401 | 0.61 | 0.76 | 58 | GOL |
| 2 | 158 | 0.51 | 0.79 | 24 | empty |
| 3 | 68 | 0.35 | 0.77 | 19 | empty |
| 4 | 102 | 0.35 | 0.74 | 24 | empty |
| 5 | 61 | 0.32 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 4125 Ų buried · 57 hydrogen bonds · protein-protein
Compared structures
- 3JTQ · Mutations in Cephalosporin Acylase Affecting Stability and Autoproteolysis · 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
- Every structure of UniProt A4ZVL3
- Elsewhere: RCSB PDB 3JTQ · PDBe 3JTQ · UniProt A4ZVL3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.