Research workbench
Crystal structure of the cell wall targeting domain of peptidylglycan hydrolase ALE-1
Analyse Crystal structure of the cell wall targeting domain of peptidylglycan hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R77
- Type
- protein
- Length
- 202 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- Staphylococcus capitis
- Molecule
- Cell Wall Targeting Domain of Glycylglycine Endopeptidase ALE-1
- EC
- 3.4.24.7
- UniProt
- O05156
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · resolution 1.75 · 2 distinct chains · 3% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell Wall Targeting Domain of Glycylglycine Endopeptidase ALE-1 (EC 3.4.24.7) | protein | 99 | 3% helix, 54% strand | O05156 |
| B | Cell Wall Targeting Domain of Glycylglycine Endopeptidase ALE-1 (EC 3.4.24.7) | protein | 103 | 3% helix, 51% strand | O05156 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.61 | 0.80 | 31 | empty |
| 2 | 63 | 0.35 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 623 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1R77 · Crystal structure of the cell wall targeting domain of peptidylglycan hydrolase ale-1 · the same entry in another collection · chain A against A, TM-score 1.00
- O05156 · AlphaFold monomer V2.0 prediction for glycyl-glycine endopeptidase ale-1 (O05156) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 O05156
- Elsewhere: RCSB PDB 1R77 · PDBe 1R77 · UniProt O05156
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