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Binding mode of azide to ferric aplysia limacina myoglobin. crystallographic analysis at 1.9 ångströms resolution

Analyse Binding mode of azide to ferric aplysia limacina myoglobin. crystallographic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MBA
Type
protein
Length
146 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Myoglobin
UniProt
P02210
Ligands
ACE, HEM, AZI
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMyoglobinprotein14676% helix, 0% strandP02210

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A
  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • AZI · Azide ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12390.730.8729AZI, HEM

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 5MBA · Binding mode of azide to ferric aplysia limacina myoglobin. crystallographic analysis at… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02210 · AlphaFold monomer V2.0 prediction for globin (P02210) · a predicted model of the same protein · chain A against A, TM-score 0.99

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