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RNase a in complex with CP4PA

Analyse RNase a in complex with CP4PA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PVW
Type
protein
Length
248 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease pancreatic
EC
4.6.1.18
UniProt
P61823
Ligands
OZV, P0J
Pockets
2 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BRibonuclease pancreatic (EC 4.6.1.18)protein12421% helix, 35% strandP61823

Ligands and binding sites

  • OZV · 5'-O-[(R)-hydroxy{[(4r,8s)-4,6,8-trihydroxy-2,4,6,8-tetraoxo-1,3,5,7,2lambda~5~,4lambda~5~,6lambda~5~, 8lambda~5~-tetroxatetraphosphocan-2-yl]oxy}phosphoryl]adenosine · ligand · chains A
  • P0J · 2,4,6,8-tetrahydroxy-1,3,5,7,2lambda~5~,4lambda~5~, 6lambda~5~,8lambda~5~-tetroxatetraphosphocane-2,4,6,8-tetrone · ligand · chains B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11480.440.7629empty
2690.360.7715empty

Interfaces

1 interface between chains.

  • A–B · 305 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

  • 6PVW · RNase A in complex with cp4pA · the same entry in another collection · chain A against A, TM-score 1.00

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