Research workbench
Crystal structures of the B1 domain of protein L from peptostreptococcus magnus with a tyrosine to tryptophan substitution
Analyse Crystal structures of the B1 domain of protein L from peptostreptococcus magnus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HZ6
- Type
- protein
- Length
- 193 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein L
- UniProt
- Q51912
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein L | protein | 67 | 31% helix, 42% strand | Q51912 |
| B, C | Protein L | protein | 63 | 33% helix, 44% strand | Q51912 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.45 | 0.84 | 19 | empty |
| 2 | 68 | 0.35 | 0.77 | 19 | empty |
Interfaces
3 interfaces between chains.
- B–C · 594 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 444 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 59 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1HZ6 · Crystal structures of the B1 domain of protein L from peptostreptococcus magnus with a… · 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 Q51912
- Elsewhere: RCSB PDB 1HZ6 · PDBe 1HZ6 · UniProt Q51912
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