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X-ray crystal structure of ferric aplysia limacina myoglobin in different liganded states

Analyse X-ray crystal structure of ferric aplysia limacina myoglobin in different… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FAL
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, CYN
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMyoglobinprotein14679% helix, 0% strandP02210

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A
  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • CYN · Cyanide 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
12140.720.8726CYN, HEM

Modifications

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

Compared structures

  • 2FAL · X-ray crystal structure of ferric aplysia limacina myoglobin in different liganded states · 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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