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Ancestral myoglobin ambwb' of basilosaurus relative (polyphyly) imidazole-ligand

Analyse Ancestral myoglobin ambwb' of basilosaurus relative (polyphyly) imidazole-ligand in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5YCJ
Type
protein
Length
311 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ancestral myoglobin ambwb' of basilosaurus relative (polyphyly)
Ligands
HEM
Pockets
4 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAncestral myoglobin ambwb' of basilosaurus relative (polyphyly)protein15475% helix, 0% strand—
BAncestral myoglobin ambwb' of basilosaurus relative (polyphyly)protein15775% helix, 0% strand—

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
  • IMD · Imidazole · additive · 2 copies · chains A, B

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
14190.690.8048empty
22090.680.8524HEM, IMD
32110.670.8425HEM, IMD
4970.350.7424empty

Interfaces

1 interface between chains.

  • A–B · 734 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 5YCJ · Ancestral myoglobin aMbWb' of Basilosaurus relative (polyphyly) imidazole-ligand · the same entry in another collection · chain A against A, TM-score 1.00

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