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MolNFT v1 · #102393 · protein

Structure of RNase as, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo

4OKE · 3'-5' exoribonuclease RV2179C/MT2234.1: “Structure of RNase as, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo”. X-ray diffraction, 2 ligands (AMP, MG), 3 pockets (best druggability 0.63). MolNFT…

PDB
4OKE
Type
protein
Length
318 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
3'-5' exoribonuclease RV2179C/MT2234.1
EC
3.1.13.-
UniProt
L7N5T0
Ligands
AMP, MG
Pockets
3 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A3'-5' exoribonuclease RV2179C/MT2234.1 (EC 3.1.13.-)protein16037% helix, 21% strandL7N5T0
B3'-5' exoribonuclease RV2179C/MT2234.1 (EC 3.1.13.-)protein15835% helix, 22% strandL7N5T0

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · 3 copies · chains A, B
  • MG · Magnesium ion · metal · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14300.630.7739AMP, MG
22750.560.7636AMP, MG
3980.430.7822empty

Interfaces

1 interface between chains.

  • A–B · 1269 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 4OKE · Structure of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial… · the same entry in another collection · chain A against A, TM-score 1.00

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