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Elephant seal myoglobin esmb

Analyse Elephant seal myoglobin esmb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DDU
Type
protein
Length
308 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Myoglobin
UniProt
R9S002
Ligands
HEM, SO4
Pockets
4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CMyoglobinprotein15475% helix, 0% strandR9S002

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, C
  • SO4 · Sulfate ion · ion · 16 copies · chains A, 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11920.690.8630HEM
21890.680.8631HEM
31600.590.8219SO4
4670.270.7212SO4

Interfaces

1 interface between chains.

  • A–C · 356 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 7DDU · Elephant seal myoglobin esMb · the same entry in another collection · chain A against A, TM-score 1.00

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