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Crystal structure of human reticulon 4 interacting protein 1 in complex with NADPH

Analyse Crystal structure of human reticulon 4 interacting protein 1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2VN8
Type
protein
Length
713 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Reticulon-4-interacting protein 1
UniProt
Q8WWV3
Ligands
NDP, NA
Pockets
3 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReticulon-4-interacting protein 1protein35836% helix, 24% strandQ8WWV3
BReticulon-4-interacting protein 1protein35537% helix, 25% strandQ8WWV3

Ligands and binding sites

  • NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
  • NA · Sodium ion · metal · chains A
  • CIT · Citric acid · additive · chains A
  • GOL · Glycerol · additive · chains 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17320.740.7968NDP
27550.730.7861NDP
37310.680.7680empty

Interfaces

1 interface between chains.

  • A–B · 637 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 2VN8 · Crystal structure of human Reticulon 4 interacting protein 1 in complex with NADPH · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8WWV3 · AlphaFold monomer V2.0 prediction for reticulon-4-interacting protein 1, mitochondrial… · a predicted model of the same protein · chain B against A, TM-score 1.00

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