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Crystal structure of Kemp Eliminase HG3 K50Q

Analyse Crystal structure of Kemp Eliminase HG3 K50Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7K4R
Type: protein
Length: 305 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.57
Source: Thermoascus aurantiacus
Molecule: Endo-1,4-beta-xylanase
EC: 3.2.1.8
UniProt: P23360
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · resolution 1.57 · 1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase (EC 3.2.1.8)	protein	305	43% helix, 20% strand	P23360

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	104	0.56	0.84	25	empty

Compared structures

7K4R · Crystal structure of kemp eliminase HG3 K50Q · the same entry in another collection · chain A against A, TM-score 1.00
P23360 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P23360) · 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 P23360
Elsewhere: RCSB PDB 7K4R · PDBe 7K4R · UniProt P23360

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