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Enzymatic and structural characterisation of amphinase, a novel cytotoxic ribonuclease from rana pipiens oocytes

Analyse Enzymatic and structural characterisation of amphinase, a novel cytotoxic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2P6Z
Type
protein
Length
221 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Recombinant amphinase-2
EC
3.1.27.-
UniProt
P85073
Ligands
NA
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARecombinant amphinase-2 (EC 3.1.27.-)protein11224% helix, 41% strandP85073
BRecombinant amphinase-2 (EC 3.1.27.-)protein10922% helix, 42% strandP85073

Ligands and binding sites

  • NA · Sodium ion · metal · 3 copies · chains A, B
  • CIT · Citric acid · additive · 3 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
17020.720.7959CIT, NA

Interfaces

1 interface between chains.

  • A–B · 658 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 2P6Z · Enzymatic and Structural Characterisation of Amphinase, a Novel Cytotoxic Ribonuclease… · the same entry in another collection · chain A against A, TM-score 1.00
  • P85073 · AlphaFold monomer V2.0 prediction for amphinase-2 (P85073) · a predicted model of the same protein · chain A against A, TM-score 0.96

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