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Crystal structure of chondroitin ABC lyase I from proteus vulgaris at 1.9 ångströms resolution

Analyse Crystal structure of chondroitin ABC lyase I from proteus vulgaris at 1.9… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HN0
Type
protein
Length
971 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chondroitin ABC lyase I
EC
4.2.2.4
UniProt
P59807
Ligands
NA
Pockets
7 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChondroitin ABC lyase I (EC 4.2.2.4)protein97127% helix, 30% strandP59807

Ligands and binding sites

  • NA · Sodium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.620.9423empty
21390.430.7626empty
3850.350.7521empty
4880.330.7422empty
5700.320.7516empty

Compared structures

  • 1HN0 · Crystal structure of chondroitin ABC lyase I from proteus vulgaris at 1.9 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
  • P59807 · AlphaFold monomer V2.0 prediction for chondroitin sulfate ABC endolyase (P59807) · a predicted model of the same protein · chain A against A, TM-score 1.00

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