MolNFT v1 · #120115 · protein
Crystal structure of chitinase-H from ostrinia furnacalis
5GPR: “Crystal structure of chitinase-H from ostrinia furnacalis”. X-ray diffraction, 1 ligand (NAG), 3 pockets (best druggability 0.71). MolNFT v1 #120115 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5GPR
- Type
- protein
- Length
- 536 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitinase
- UniProt
- Q4AE59
- Ligands
- NAG
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitinase | protein | 536 | 27% helix, 27% strand | Q4AE59 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 560 | 0.71 | 0.80 | 57 | empty |
| 2 | 68 | 0.33 | 0.76 | 17 | empty |
| 3 | 66 | 0.31 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 2 glycan, 1 disulfide (N-glycosylation, disulfide).
Compared structures
- 5GPR · Crystal structure of chitinase-h from Ostrinia furnacalis · 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 Q4AE59
- Elsewhere: RCSB PDB 5GPR · PDBe 5GPR · UniProt Q4AE59
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