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MolNFT v2 · #14831 · protein

1MLQ: Structural and functional effects of apolar mutations of VAL68(E11) in myoglobin

1MLQ: “Structural and functional effects of apolar mutations of VAL68(E11) in myoglobin”. X-ray diffraction at 2, 3 ligands (HEM, SO4, CMO), 1 pocket (best druggability 0.72). MolNFT v2 #14831 on GenesisL1: 3D structure, binding sites and…

3D structure of 1MLQ: Structural and functional effects of apolar mutations of VAL68(E11) in myoglobin (MolNFT v2 / PDB Bank)
3D structure of 1MLQ: Structural and functional effects of apolar mutations of VAL68(E11) in myoglobin (MolNFT v2 / PDB Bank)
PDB
1MLQ
Type
protein
Length
154 residues
Chains
1
Method
x-ray diffraction
Authors
Quillin, M.L., Phillips Jr., G.N.
Deposited
06/15/94
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Physeter catodon
Molecule
Myoglobin
UniProt
P02185
Ligands
HEM, SO4, CMO
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMyoglobinprotein15479% helix, 0% strandP02185

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • SO4 · Sulfate ion · ion · chains A
  • CMO · Carbon monoxide · 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
12220.720.8729HEM, CMO

Compared structures

  • 1MLQ · Structural and functional effects of apolar mutations of VAL68(E11) in myoglobin · the same entry in another collection · chain A against A, TM-score 1.00
  • P02185 · AlphaFold monomer V2.0 prediction for myoglobin (P02185) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Other records of 1MLQ

  • 1MLQ-2 · MolNFT v1 / PDB · Structural and functional effects of apolar mutations of VAL68(E11) in myoglobin

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