MolNFT v1 · #88808 · protein
Crystal structure of a family 98 glycoside hydrolase catalytic module (SP3GH98) (L19 mutant)
4D6C: “Crystal structure of a family 98 glycoside hydrolase catalytic module (SP3GH98) (L19 mutant)”. X-ray diffraction, 4 pockets (best druggability 0.60). MolNFT v1 #88808 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4D6C
- Type
- protein
- Length
- 586 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase
- EC
- 3.2.1.102
- UniProt
- A5LBQ0
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoside hydrolase (EC 3.2.1.102) | protein | 586 | 32% helix, 25% strand | A5LBQ0 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.60 | 0.79 | 36 | empty |
| 2 | 88 | 0.57 | 0.86 | 18 | empty |
| 3 | 123 | 0.50 | 0.80 | 25 | empty |
| 4 | 71 | 0.33 | 0.75 | 16 | empty |
Compared structures
- 4D6C · Crystal structure of a family 98 glycoside hydrolase catalytic module (Sp3GH98)(L19… · 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 A5LBQ0
- Elsewhere: RCSB PDB 4D6C · PDBe 4D6C · UniProt A5LBQ0
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