Research workbench
Crystal structure of ep complex of catalytic-site mutant xylanase from streptomyces olivaceoviridis E-86
Analyse Crystal structure of ep complex of catalytic-site mutant xylanase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D23
- Type
- protein
- Length
- 854 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-D-xylanase
- EC
- 3.2.1.8
- UniProt
- Q7SI98
- Ligands
- XYS, AZI
- Pockets
- 9 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Endo-1,4-beta-D-xylanase (EC 3.2.1.8) | protein | 427 | 33% helix, 24% strand | Q7SI98 |
Ligands and binding sites
- XYS · alpha-D-xylopyranose · sugar · 4 copies · chains A, B
- AZI · Azide ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.67 | 0.80 | 50 | empty |
| 2 | 90 | 0.38 | 0.76 | 19 | XYS, AZI, GOL |
| 3 | 50 | 0.36 | 0.80 | 15 | empty |
| 4 | 120 | 0.36 | 0.73 | 22 | empty |
| 5 | 70 | 0.34 | 0.76 | 19 | XYS, AZI |
Interfaces
1 interface between chains.
- A–B · 1027 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 2D23 · Crystal structure of EP complex of catalytic-site mutant xylanase from Streptomyces… · 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 Q7SI98
- Elsewhere: RCSB PDB 2D23 · PDBe 2D23 · UniProt Q7SI98
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