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The glucuronoyl esterase OTCE15A R268A variant from opitutus terrae in complex with, and covalently linked to, D-glucuronate
Analyse The glucuronoyl esterase OTCE15A R268A variant from opitutus terrae in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B7H
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative acetyl xylan esterase
- UniProt
- B1ZMF4
- Ligands
- GLY, GCU, NA
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative acetyl xylan esterase | protein | 370 | 39% helix, 21% strand | B1ZMF4 |
Ligands and binding sites
- GLY · Glycine · ligand · 4 copies · chains A
- GCU · alpha-D-glucopyranuronic acid · sugar · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 12 copies · chains A
- DMS · Dimethyl sulfoxide · additive · 11 copies · chains A
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 | 157 | 0.52 | 0.80 | 27 | EDO |
| 2 | 66 | 0.37 | 0.77 | 15 | empty |
| 3 | 71 | 0.36 | 0.77 | 20 | GCU, DMS, EDO |
Modifications
Observed in the structure: 1 glycan (O-glycosylation).
Compared structures
- 7B7H · The glucuronoyl esterase OtCE15A R268A variant from Opitutus terrae in complex with, and… · 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 B1ZMF4
- Elsewhere: RCSB PDB 7B7H · PDBe 7B7H · UniProt B1ZMF4
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