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Crystal structure of a thermostable mutant of the catalytic domain of GH19 chitinase from gazyumaru, ficus microcarpa
Analyse Crystal structure of a thermostable mutant of the catalytic domain of GH19… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V92
- Type
- protein
- Length
- 975 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GH19 chitinase
- EC
- 3.2.1.14
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | GH19 chitinase (EC 3.2.1.14) | protein | 243 | 45% helix, 2% strand | — |
| B | GH19 chitinase (EC 3.2.1.14) | protein | 244 | 43% helix, 2% strand | — |
| D | GH19 chitinase (EC 3.2.1.14) | protein | 245 | 43% helix, 2% strand | — |
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 862 | 0.74 | 0.78 | 87 | empty |
| 2 | 739 | 0.73 | 0.79 | 65 | empty |
| 3 | 642 | 0.73 | 0.80 | 61 | empty |
| 4 | 716 | 0.72 | 0.79 | 65 | empty |
| 5 | 258 | 0.54 | 0.76 | 37 | empty |
Interfaces
5 interfaces between chains.
- C–D · 724 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 697 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 291 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 252 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 171 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 7V92 · Crystal Structure of a thermostable mutant of the Catalytic Domain of GH19 Chitinase from… · 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
- Elsewhere: RCSB PDB 7V92 · PDBe 7V92
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