Research workbench
Lytic transglycosylase in action
Analyse Lytic transglycosylase in action in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O29
- Type
- protein
- Length
- 576 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transglycosylase
- EC
- 4.2.2.-
- UniProt
- A0A0Y5YPU4
- Pockets
- 7 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transglycosylase (EC 4.2.2.-) | protein | 576 | 67% helix, 1% strand | A0A0Y5YPU4 |
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.46 | 0.75 | 27 | empty |
| 2 | 165 | 0.43 | 0.74 | 33 | empty |
| 3 | 130 | 0.41 | 0.75 | 24 | empty |
| 4 | 94 | 0.39 | 0.76 | 14 | empty |
| 5 | 73 | 0.32 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5O29 · Lytic transglycosylase in action · 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 A0A0Y5YPU4
- Elsewhere: RCSB PDB 5O29 · PDBe 5O29 · UniProt A0A0Y5YPU4
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