Research workbench
Crystal structure of mycobacterium tuberculosis L,D-transpeptidase LDTMT2 N55 truncation mutant (resideus 55-408)
Analyse Crystal structure of mycobacterium tuberculosis L,D-transpeptidase LDTMT2 N55… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VYN
- Type
- protein
- Length
- 696 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable conserved lipoprotein lpps
- EC
- 2.3.2.12
- UniProt
- O53223
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable conserved lipoprotein lpps (EC 2.3.2.12) | protein | 347 | 9% helix, 44% strand | O53223 |
| B | Probable conserved lipoprotein lpps (EC 2.3.2.12) | protein | 349 | 9% helix, 42% strand | O53223 |
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 664 | 0.71 | 0.78 | 48 | empty |
| 2 | 107 | 0.49 | 0.81 | 20 | empty |
| 3 | 77 | 0.46 | 0.82 | 19 | empty |
| 4 | 87 | 0.43 | 0.79 | 18 | empty |
| 5 | 123 | 0.42 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 394 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3VYN · Crystal structure of Mycobacterium tuberculosis L,D-transpeptidase LdtMt2 N55 truncation… · the same entry in another collection · chain A against A, TM-score 1.00
- O53223 · AlphaFold monomer V2.0 prediction for L,D-transpeptidase 2 (O53223) · a predicted model of the same protein · 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 O53223
- Elsewhere: RCSB PDB 3VYN · PDBe 3VYN · UniProt O53223
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