Research workbench
Crystal structure of CBXYN10B from caldicellulosiruptor bescii and its MUTANT(E139A) in complex with hydrolyzed xylotetraose
Analyse Crystal structure of CBXYN10B from caldicellulosiruptor bescii and its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PMD
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase
- EC
- 3.2.1.8
- UniProt
- B9MMA5
- Ligands
- XYP
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase (EC 3.2.1.8) | protein | 329 | 40% helix, 20% strand | B9MMA5 |
Ligands and binding sites
- XYP · beta-D-xylopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.60 | 0.79 | 32 | XYP |
| 2 | 62 | 0.31 | 0.75 | 15 | empty |
Compared structures
- 4PMD · Crystal structure of CbXyn10B from Caldicellulosiruptor bescii and its mutant(E139A) in… · 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 B9MMA5
- Elsewhere: RCSB PDB 4PMD · PDBe 4PMD · UniProt B9MMA5
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