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Crystal Structure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris in apo form

Analyse Crystal Structure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KPL
Type: protein
Length: 294 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.75
Source: Cordyceps militaris CM01
Molecule: Chitinase
UniProt: G3JPF7
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · resolution 1.75 · 1 distinct chain · 40% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase	protein	294	40% helix, 17% strand	G3JPF7

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
PGE · Triethylene glycol · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.32	0.76	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6KPL · Crystal structure of endo-beta-N-acetylglucosaminidase from cordyceps militaris in apo… · the same entry in another collection · 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 G3JPF7
Elsewhere: RCSB PDB 6KPL · PDBe 6KPL · UniProt G3JPF7

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