MolNFT v1 · #1803 · protein
Mutational and crystallographic analyses of the active site residues of the bacillus circulans xylanase
1BCX: “Mutational and crystallographic analyses of the active site residues of the bacillus circulans xylanase”. X-ray diffraction, 2 ligands (XYP, SO4), 1 pocket (best druggability 0.57). MolNFT v1 #1803 on GenesisL1: 3D structure…
- PDB
- 1BCX
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xylanase
- EC
- 3.2.1.8
- UniProt
- P09850
- Ligands
- XYP, SO4
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylanase (EC 3.2.1.8) | protein | 185 | 5% helix, 62% strand | P09850 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.57 | 0.80 | 27 | XYP |
Compared structures
- 1BCX · Mutational and crystallographic analyses of the active site residues of the bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- P09850 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P09850) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P09850
- Elsewhere: RCSB PDB 1BCX · PDBe 1BCX · UniProt P09850
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