MolNFT v1 · #93460 · protein
Feruloyl esterase domain of xyny from clostridium thermocellum before exposure to 266NM UV laser
4H35 · Endo-1,4-beta-xylanase Y: “Feruloyl esterase domain of xyny from clostridium thermocellum before exposure to 266NM UV laser”. X-ray diffraction, 1 ligand (CD), 8 pockets (best druggability 0.55). MolNFT v1 #93460 on GenesisL1: 3D…
- PDB
- 4H35
- Type
- protein
- Length
- 566 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase Y
- EC
- 3.2.1.8
- UniProt
- P51584
- Ligands
- CD
- Pockets
- 8 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Endo-1,4-beta-xylanase Y (EC 3.2.1.8) | protein | 283 | 33% helix, 20% strand | P51584 |
Ligands and binding sites
- CD · Cadmium ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.55 | 0.81 | 27 | empty |
| 2 | 165 | 0.55 | 0.81 | 27 | empty |
| 3 | 52 | 0.41 | 0.82 | 18 | empty |
| 4 | 56 | 0.38 | 0.80 | 17 | empty |
| 5 | 83 | 0.38 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1141 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered, phosphorylation).
Compared structures
- 4H35 · Feruloyl Esterase Domain of XYNY from Clostridium thermocellum before exposure to 266nm… · the same entry in another collection · chain A against A, TM-score 1.00
- P51584 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Y (P51584) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P51584
- Elsewhere: RCSB PDB 4H35 · PDBe 4H35 · UniProt P51584
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