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Crystal structure of the RHSP2 C-terminal toxin domain in complex with its immunity protein, RHSI2

Analyse Crystal structure of the RHSP2 C-terminal toxin domain in complex with its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RT7
Type
protein
Length
1,718 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RHSP2; RHSI2
UniProt
A0A0H2Z8A2, A0A367GXM0
Pockets
20 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 25% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, E, G, KRHSP2protein14330% helix, 29% strandA0A0H2Z8A2
D, C, F, H, J, LRHSI2protein14422% helix, 35% strandA0A367GXM0
IRHSP2protein13924% helix, 29% strandA0A0H2Z8A2

Ligands and binding sites

  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains A, D, B, C

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

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13840.590.7633empty
23030.580.7737empty
33930.570.7545empty
41910.540.7832empty
52900.530.7533empty

Interfaces

14 interfaces between chains.

  • A–D · 1243 Ų buried · 28 hydrogen bonds · protein-protein
  • I–J · 1225 Ų buried · 29 hydrogen bonds · protein-protein
  • B–C · 1216 Ų buried · 26 hydrogen bonds · protein-protein
  • G–H · 1197 Ų buried · 28 hydrogen bonds · protein-protein
  • E–F · 1183 Ų buried · 31 hydrogen bonds · protein-protein

Compared structures

  • 7RT7 · Crystal structure of the RhsP2 C-terminal toxin domain in complex with its immunity… · the same entry in another collection · chain A against A, TM-score 1.00

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