Research workbench
Crystal structure of streptococcus pneumoniae hyaluronate lyase from 30PERCENT pegmme.
Analyse Crystal structure of streptococcus pneumoniae hyaluronate lyase from 30PERCENT… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BRW
- Type
- protein
- Length
- 1,442 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hyaluronate lyase
- EC
- 4.2.2.1
- UniProt
- Q54873
- Ligands
- SO4
- Pockets
- 19 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hyaluronate lyase (EC 4.2.2.1) | protein | 721 | 36% helix, 27% strand | Q54873 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.71 | 0.99 | 21 | empty |
| 2 | 706 | 0.70 | 0.77 | 69 | empty |
| 3 | 55 | 0.70 | 0.98 | 22 | empty |
| 4 | 600 | 0.65 | 0.76 | 63 | empty |
| 5 | 355 | 0.60 | 0.77 | 42 | empty |
Interfaces
1 interface between chains.
- A–B · 348 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2BRW · Crystal structure of Streptococcus Pneumoniae Hyaluronate Lyase from 30percent PEGMME. · the same entry in another collection · chain A against A, TM-score 1.00
- Q54873 · AlphaFold monomer V2.0 prediction for hyaluronate lyase (Q54873) · 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 Q54873
- Elsewhere: RCSB PDB 2BRW · PDBe 2BRW · UniProt Q54873
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