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Crystal structure of hexacoordinated heme protein from anhydrobiotic tardigrade at pH 4

Analyse Crystal structure of hexacoordinated heme protein from anhydrobiotic tardigrade… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZIQ
Type
protein
Length
617 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Globin protein
UniProt
A0A1D1V896
Ligands
HEM, SO4
Pockets
4 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CGlobin proteinprotein15580% helix, 0% strandA0A1D1V896
DGlobin proteinprotein15280% helix, 0% strandA0A1D1V896

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
  • SO4 · Sulfate ion · ion · 7 copies · chains A, C, B
  • EDO · 1,2-ethanediol · additive · 3 copies · chains A, B, C

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14760.820.8872HEM
27440.800.8377HEM
34850.750.8347empty
41840.700.8723HEM

Interfaces

5 interfaces between chains.

  • A–B · 851 Ų buried · 19 hydrogen bonds · protein-protein
  • C–D · 824 Ų buried · 18 hydrogen bonds · protein-protein
  • B–C · 340 Ų buried · 12 hydrogen bonds · protein-protein
  • A–D · 282 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 275 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5ZIQ · Crystal structure of hexacoordinated heme protein from anhydrobiotic tardigrade at pH 4 · the same entry in another collection · chain A against A, TM-score 1.00

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