Research workbench
The structure of mutant (N93Q) of bla G 2
Analyse The structure of mutant (N93Q) of bla G 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YG9
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartic protease bla G 2
- EC
- 3.4.23.-
- UniProt
- P54958
- Ligands
- NAG, ZN
- Pockets
- 4 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartic protease bla G 2 (EC 3.4.23.-) | protein | 330 | 13% helix, 48% strand | P54958 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.45 | 0.74 | 22 | empty |
| 2 | 128 | 0.41 | 0.75 | 22 | empty |
| 3 | 93 | 0.39 | 0.77 | 19 | empty |
| 4 | 93 | 0.34 | 0.74 | 23 | empty |
Modifications
Observed in the structure: 5 disulfide, 2 glycan, 1 modified (disulfide, N-glycosylation, oxidation).
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 P54958
- Elsewhere: RCSB PDB 1YG9 · PDBe 1YG9 · UniProt P54958
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