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… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HZ5
- 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
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 · 10 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 170 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1HZ5 · 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 1HZ5 · PDBe 1HZ5 · UniProt Q51912
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