Research workbench
Crystal structure of class I chitinase from oryza sativa L. japonica
Analyse Crystal structure of class I chitinase from oryza sativa L. japonica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IWR
- Type
- protein
- Length
- 490 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitinase
- EC
- 3.2.1.14
- UniProt
- Q7DNA1
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitinase (EC 3.2.1.14) | protein | 244 | 44% helix, 3% strand | Q7DNA1 |
| B | Chitinase (EC 3.2.1.14) | protein | 246 | 44% helix, 3% strand | Q7DNA1 |
Ligands and binding sites
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.62 | 0.76 | 47 | MES |
| 2 | 496 | 0.60 | 0.74 | 41 | MES |
Interfaces
1 interface between chains.
- A–B · 533 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 Q7DNA1
- Elsewhere: RCSB PDB 3IWR · PDBe 3IWR · UniProt Q7DNA1
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