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Human U1A protein with F37M and F77M mutations for improved phasing

Analyse Human U1A protein with F37M and F77M mutations for improved phasing in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LHX
Type
protein
Length
96 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
U1 small nuclear ribonucleoprotein a
UniProt
P09012
Ligands
NA
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AU1 small nuclear ribonucleoprotein aprotein9632% helix, 25% strandP09012

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • ACT · Acetate ion · additive · 2 copies · chains A
  • BME · Beta-mercaptoethanol · additive · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1530.330.7815ACT

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 7LHX · Human U1A protein with F37M and F77M mutations for improved phasing · the same entry in another collection · chain A against A, TM-score 1.00

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