Research workbench
L,D-transpeptidase from klebsiella pneumoniae
Analyse L,D-transpeptidase from klebsiella pneumoniae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LZH
- Type
- protein
- Length
- 278 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L,D-transpeptidase
- UniProt
- A6T6R4
- Pockets
- 4 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L,D-transpeptidase | protein | 278 | 21% helix, 26% strand | A6T6R4 |
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 | 117 | 0.48 | 0.79 | 18 | empty |
| 2 | 199 | 0.47 | 0.75 | 25 | empty |
| 3 | 51 | 0.38 | 0.81 | 14 | empty |
| 4 | 60 | 0.28 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4LZH · L,D-transpeptidase from Klebsiella pneumoniae · 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 A6T6R4
- Elsewhere: RCSB PDB 4LZH · PDBe 4LZH · UniProt A6T6R4
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