Research workbench
Structure of endo-1,4-beta-xylanase C
Analyse Structure of endo-1,4-beta-xylanase C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UKR
- Type
- protein
- Length
- 724 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-B-xylanase I
- EC
- 3.2.1.8
- UniProt
- P55329
- Pockets
- 7 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Endo-1,4-B-xylanase I (EC 3.2.1.8) | protein | 181 | 8% helix, 60% strand | P55329 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.58 | 0.79 | 39 | empty |
| 2 | 184 | 0.54 | 0.79 | 33 | empty |
| 3 | 173 | 0.53 | 0.79 | 28 | empty |
| 4 | 165 | 0.46 | 0.75 | 25 | empty |
| 5 | 85 | 0.41 | 0.78 | 16 | empty |
Interfaces
3 interfaces between chains.
- B–C · 505 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 485 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 476 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 P55329
- Elsewhere: RCSB PDB 1UKR · PDBe 1UKR · UniProt P55329
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