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Crystal structure of potassium induced heme modification in yak lactoperoxidase at 2.30 a resolution

Analyse Crystal structure of potassium induced heme modification in yak lactoperoxidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6L32
Type
protein
Length
595 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lactoperoxidase
UniProt
L8ICE9
Ligands
HEM, NAG, K, CA, ZN
Pockets
6 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALactoperoxidaseprotein59538% helix, 10% strandL8ICE9

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
  • K · Potassium ion · metal · 2 copies · chains A
  • CA · Calcium ion · metal · chains A
  • ZN · Zinc ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110300.820.8395HEM, K
2740.460.8220empty
31250.450.7730empty
4510.370.8017empty
5750.350.7618empty

Modifications

Observed in the structure: 7 disulfide, 4 glycan, 2 cofactor (disulfide, N-glycosylation, heme attachment).

Compared structures

  • 6L32 · Crystal structure of potassium induced heme modification in yak lactoperoxidase at 2.30 A… · the same entry in another collection · chain A against A, TM-score 1.00

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