GL1X · GenesisL1 explorer

MolNFT v1 · #40013 · protein

Escherichia COLI RNase II

2ID0 · Exoribonuclease 2: “Escherichia COLI RNase II”. X-ray diffraction, 1 ligand (MN), 20 pockets (best druggability 0.72). MolNFT v1 #40013 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
2ID0
Type
protein
Length
2,544 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Exoribonuclease 2
EC
3.1.13.1
UniProt
P30850
Ligands
MN
Pockets
20 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DExoribonuclease 2 (EC 3.1.13.1)protein63629% helix, 29% strandP30850

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17760.720.7867MN
26780.700.7765empty
35510.690.7970empty
49010.690.7575empty
57400.680.7682empty

Interfaces

4 interfaces between chains.

  • A–B · 694 Ų buried · 14 hydrogen bonds · protein-protein
  • A–C · 136 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 52 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 38 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 56 modified (engineered).

Compared structures

  • 2ID0 · Escherichia coli RNase II · the same entry in another collection · chain A against A, TM-score 1.00
  • P30850 · AlphaFold monomer V2.0 prediction for exoribonuclease 2 (P30850) · a predicted model of the same protein · chain A against A, TM-score 0.98

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