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Crystal structure of MCPIP1 conserved domain with magnesium ion in the catalytic center

Analyse Crystal structure of MCPIP1 conserved domain with magnesium ion in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3V34
Type
protein
Length
315 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease ZC3H12A
EC
3.1.-.-
UniProt
Q5D1E8
Ligands
MG
Pockets
1 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibonuclease ZC3H12A (EC 3.1.-.-)protein15741% helix, 21% strandQ5D1E8
BRibonuclease ZC3H12A (EC 3.1.-.-)protein15841% helix, 20% strandQ5D1E8

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B

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
15170.690.7836empty

Interfaces

1 interface between chains.

  • A–B · 240 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 3V34 · Crystal structure of MCPIP1 conserved domain with magnesium ion in the catalytic center · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5D1E8 · AlphaFold monomer V2.0 prediction for endoribonuclease ZC3H12A (Q5D1E8) · a predicted model of the same protein · chain B against A, TM-score 0.98

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