Research workbench
A CE15 glucuronoyl esterase from teredinibacter turnerae T7901
Analyse A CE15 glucuronoyl esterase from teredinibacter turnerae T7901 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HSW
- Type
- protein
- Length
- 1,262 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbohydrate esterase family 15 domain protein
- UniProt
- C5BN23
- Ligands
- BR
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbohydrate esterase family 15 domain protein | protein | 422 | 40% helix, 16% strand | C5BN23 |
| B, C | Carbohydrate esterase family 15 domain protein | protein | 420 | 40% helix, 16% strand | C5BN23 |
Ligands and binding sites
- BR · Bromide ion · ion · 2 copies · chains B, C
- EDO · 1,2-ethanediol · additive · 20 copies · chains A, B, C
- GOL · Glycerol · additive · 13 copies · chains A, B, C
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A, B, C
- PEG · Di(hydroxyethyl)ether · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1198 | 0.84 | 0.85 | 146 | GOL, EDO |
| 2 | 566 | 0.76 | 0.83 | 50 | empty |
| 3 | 227 | 0.66 | 0.83 | 25 | EDO |
| 4 | 148 | 0.62 | 0.85 | 26 | GOL |
| 5 | 234 | 0.54 | 0.77 | 33 | 1PE, GOL |
Interfaces
3 interfaces between chains.
- B–C · 1376 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 445 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 66 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 6HSW · A CE15 glucuronoyl esterase from Teredinibacter turnerae T7901 · 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 C5BN23
- Elsewhere: RCSB PDB 6HSW · PDBe 6HSW · UniProt C5BN23
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