MolNFT v1 · #154945 · protein
Crystal structure of GH30 xylanase B from talaromyces cellulolyticus expressed by pichia pastoris
6KRL · Mating factor ALPHA,GH30 xylanase B: “Crystal structure of GH30 xylanase B from talaromyces cellulolyticus expressed by pichia pastoris”. X-ray diffraction, 3 ligands (NAG, MAN, BMA), 2 pockets (best druggability 0.35). MolNFT v1…
- PDB
- 6KRL
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mating factor ALPHA,GH30 xylanase B
- UniProt
- P25501, A0A4V8H018
- Ligands
- NAG, MAN, BMA
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mating factor ALPHA,GH30 xylanase B | protein | 454 | 23% helix, 28% strand | P25501, A0A4V8H018 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
- GOL · Glycerol · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.35 | 0.75 | 15 | GOL |
| 2 | 52 | 0.26 | 0.73 | 14 | empty |
Modifications
Observed in the structure: 5 glycan, 2 disulfide (N-glycosylation, disulfide).
Compared structures
- 6KRL · Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia… · the same entry in another collection · chain A against A, TM-score 1.00
- P25501 · AlphaFold monomer V2.0 prediction for mating factor alpha (P25501) · a predicted model of the same protein · chain A against A, TM-score 0.11
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 P25501
- Every structure of UniProt A0A4V8H018
- Elsewhere: RCSB PDB 6KRL · PDBe 6KRL · UniProt P25501 · UniProt A0A4V8H018
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