MolNFT v1 · #98690 · protein
Structure of chitinase D from serratia proteamaculans revealed an unusually constrained substrate binding site
4LGX · Glycoside hydrolase family 18: “Structure of chitinase D from serratia proteamaculans revealed an unusually constrained substrate binding site”. X-ray diffraction, 3 pockets (best druggability 0.66). MolNFT v1 #98690 on GenesisL1…
- PDB
- 4LGX
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase family 18
- EC
- 3.2.1.14
- UniProt
- A8GFD6
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoside hydrolase family 18 (EC 3.2.1.14) | protein | 398 | 37% helix, 20% strand | A8GFD6 |
Ligands and binding sites
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 | 325 | 0.66 | 0.81 | 39 | ACT, GOL |
| 2 | 100 | 0.43 | 0.78 | 22 | GOL |
| 3 | 68 | 0.31 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 4LGX · Structure of Chitinase D from Serratia proteamaculans revealed an unusually constrained… · 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 A8GFD6
- Elsewhere: RCSB PDB 4LGX · PDBe 4LGX · UniProt A8GFD6
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