Research workbench
Monomeric protein L B1 domain with a G15A mutation
Analyse Monomeric protein L B1 domain with a G15A mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K53
- Type
- protein
- Length
- 144 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein L
- UniProt
- Q51912
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein L | protein | 72 | 31% helix, 39% strand | Q51912 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.36 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 138 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1K53 · Monomeric Protein L B1 Domain with a G15A Mutation · 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 1K53 · PDBe 1K53 · UniProt Q51912
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