Research workbench
2.1 a resolution structure of escherichia COLI lytic transglycoyslase SLT35 in complex with calcium
Analyse 2.1 a resolution structure of escherichia COLI lytic transglycoyslase SLT35 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QDT
- Type
- protein
- Length
- 312 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Escherichia coli
- Molecule
- Lytic murein transglycosylase B
- UniProt
- P41052
- Ligands
- CA
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lytic murein transglycosylase B | protein | 312 | 50% helix, 11% strand | P41052 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 284 | 0.51 | 0.74 | 35 | EDO, GOL |
| 2 | 54 | 0.31 | 0.76 | 15 | empty |
Compared structures
- 1QDT · 2.1 a resolution structure of escherichia COLI lytic transglycoyslase SLT35 in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P41052 · AlphaFold monomer V2.0 prediction for membrane-bound lytic murein transglycosylase B… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P41052
- Elsewhere: RCSB PDB 1QDT · PDBe 1QDT · UniProt P41052
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