Research workbench
Crystal structure of lysm domain from volvox carteri chitinase
Analyse Crystal structure of lysm domain from volvox carteri chitinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5K2L
- Type
- protein
- Length
- 49 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitinase, lysozyme
- UniProt
- D8UFB5
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitinase, lysozyme | protein | 49 | 31% helix, 16% strand | D8UFB5 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5K2L · Crystal structure of LysM domain from Volvox carteri chitinase · 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 D8UFB5
- Elsewhere: RCSB PDB 5K2L · PDBe 5K2L · UniProt D8UFB5
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