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The determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement

Analyse The determination of the crystal structure of recombinant pig myoglobin by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1PMB
Type
protein
Length
306 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Myoglobin
UniProt
P02189
Ligands
HEM
Pockets
2 · best druggability 0.71

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMyoglobinprotein15376% helix, 0% strandP02189

Ligands and binding sites

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

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.710.8727HEM
22000.710.8726HEM

Compared structures

  • 1PMB · The determination of the crystal structure of recombinant pig myoglobin by molecular… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02189 · AlphaFold monomer V2.0 prediction for myoglobin (P02189) · a predicted model of the same protein · chain A against A, TM-score 0.99

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