Research workbench
Crystal Structure of Keratinicyclin B
Analyse Crystal Structure of Keratinicyclin B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LTB
- Type
- protein
- Length
- 12 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 0.95
- Source
- Amycolatopsis keratiniphila
- Molecule
- Keratinicyclin B peptide moiety
- Ligands
- YBJ, BGC, Z6G, MAN
Structure
x-ray diffraction · resolution 0.95 · 1 distinct chain · 0% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Keratinicyclin B peptide moiety | protein | 6 | 0% helix, 17% strand | — |
Ligands and binding sites
- YBJ · (2~{S},4~{S},5~{R},6~{S})-4-azanyl-5-methoxy-6-methyl-oxan-2-ol · ligand · 2 copies · chains A, B
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
- Z6G · 3-ammonio-2,3,6-trideoxy-alpha-L-arabino-hexopyranose · sugar · 2 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A, B
- FMT · Formic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 201 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified, 4 glycan, 2 covalent (nonstandard, glycosylation, covalent ligand).
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7LTB · PDBe 7LTB
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