MolNFT v1 · #34807 · protein

Crystal structure of reducing-end-xylose releasing exo-oligoxylanase D263C mutant

2DRO · Xylanase Y: “Crystal structure of reducing-end-xylose releasing exo-oligoxylanase D263C mutant”. X-ray diffraction, 1 ligand (NI), 2 pockets (best druggability 0.60). MolNFT v1 #34807 on GenesisL1: 3D structure, binding sites and…

PDB: 2DRO
Type: protein
Length: 376 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylanase Y
EC: 3.2.1.156
UniProt: Q9KB30
Ligands: NI
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylanase Y (EC 3.2.1.156)	protein	376	51% helix, 8% strand	Q9KB30

Ligands and binding sites

NI · Nickel (II) ion · metal · chains A
GOL · Glycerol · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	266	0.60	0.79	33	GOL
2	57	0.42	0.82	16	empty

Compared structures

2DRO · Crystal structure of reducing-end-xylose releasing exo-oligoxylanase D263C mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q9KB30 · AlphaFold monomer V2.0 prediction for reducing end xylose-releasing exo-oligoxylanase… · a predicted model of the same protein · chain A against A, TM-score 1.00

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 Q9KB30
Elsewhere: RCSB PDB 2DRO · PDBe 2DRO · UniProt Q9KB30

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