MolNFT v1 · #110250 · protein
X-ray structure analysis of xylanase-N44E with mes at PH6.0
4XQW · Endo-1,4-beta-xylanase 2: “X-ray structure analysis of xylanase-N44E with mes at PH6.0”. X-ray diffraction, 1 ligand (IOD), 1 pocket (best druggability 0.50). MolNFT v1 #110250 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4XQW
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase 2
- EC
- 3.2.1.8
- UniProt
- P36217
- Ligands
- IOD
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase 2 (EC 3.2.1.8) | protein | 189 | 5% helix, 61% strand | P36217 |
Ligands and binding sites
- IOD · Iodide ion · ion · 5 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.50 | 0.76 | 30 | MES |
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 P36217
- Elsewhere: RCSB PDB 4XQW · PDBe 4XQW · UniProt P36217
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