MolNFT v2 · #220005 · protein
Xenopus laevis hyaluronan synthase 1
8SMM: “Xenopus laevis hyaluronan synthase 1”. Electron microscopy at 3.2, 10 pockets (best druggability 0.87). MolNFT v2 #220005 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8SMM
- Type
- protein
- Length
- 738 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.2
- Source
- Homo sapiens; Xenopus laevis
- Molecule
- Hyaluronan synthase 1; Fab15 heavy chain; Fab15 light chain
- EC
- 2.4.1.212
- UniProt
- P13563
- Pockets
- 10 · best druggability 0.87
Structure
electron microscopy · resolution 3.2 · 3 distinct chains · 46% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hyaluronan synthase 1 (EC 2.4.1.212) | protein | 508 | 64% helix, 11% strand | P13563 |
| H | Fab15 heavy chain | protein | 124 | 5% helix, 49% strand | — |
| L | Fab15 light chain | protein | 106 | 3% helix, 49% strand | — |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 957 | 0.87 | 0.88 | 89 | empty |
| 2 | 207 | 0.52 | 0.77 | 28 | empty |
| 3 | 130 | 0.48 | 0.78 | 18 | empty |
| 4 | 116 | 0.47 | 0.79 | 15 | empty |
| 5 | 134 | 0.45 | 0.77 | 31 | empty |
Interfaces
3 interfaces between chains.
- H–L · 857 Ų buried · 3 hydrogen bonds · protein-protein
- A–H · 661 Ų buried · 6 hydrogen bonds · protein-protein
- A–L · 118 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- P13563 · AlphaFold monomer V2.0 prediction for hyaluronan synthase 1 (P13563) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P13563
- Elsewhere: RCSB PDB 8SMM · PDBe 8SMM · UniProt P13563
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