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Crystal structure of chitinase D from serratia proteamaculans at 1.45 ångström resolution

Analyse Crystal structure of chitinase D from serratia proteamaculans at 1.45 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NZC
Type
protein
Length
398 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycoside hydrolase family 18
EC
3.2.1.14
UniProt
A8GFD6
Pockets
2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycoside hydrolase family 18 (EC 3.2.1.14)protein39837% helix, 20% strandA8GFD6

Ligands and binding sites

  • GOL · Glycerol · additive · 3 copies · chains A
  • ACT · Acetate ion · additive · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12840.660.8236ACT, GOL
2920.420.7822GOL

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 4NZC · Crystal structure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00

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