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Solid-state mas NMR structure of the dimer crh

Analyse Solid-state mas NMR structure of the dimer crh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2RLZ
Type
protein
Length
170 residues
Chains
2
Method
solid-state nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hpr-like protein crh
UniProt
O06976
Pockets
2 · best druggability 0.71

Structure

solid-state nmr · 1 distinct chain · 33% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHpr-like protein crhprotein8533% helix, 19% strandO06976

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11490.710.9041empty
21300.700.9029empty

Interfaces

1 interface between chains.

  • A–B · 1736 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 2RLZ · Solid-State MAS NMR structure of the dimer Crh · the same entry in another collection · chain A against A, TM-score 1.00
  • O06976 · AlphaFold monomer V2.0 prediction for hpr-like protein crh (O06976) · a predicted model of the same protein · chain A against A, TM-score 0.68

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