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Crystal structure of the signaling protein complex 5

Analyse Crystal structure of the signaling protein complex 5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IXZ
Type
protein
Length
364 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ALR2278 protein
UniProt
Q8YUQ7
Ligands
HEM
Pockets
4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BALR2278 proteinprotein18253% helix, 16% strandQ8YUQ7

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
  • DMS · Dimethyl sulfoxide · additive · 2 copies · chains A, B
  • MLI · Malonate ion · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13520.840.9337HEM, DMS
25790.830.8882HEM, DMS, MLI
32180.570.7926empty
41320.550.8235empty

Interfaces

1 interface between chains.

  • A–B · 1107 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 5IXZ · Crystal structure of the signaling protein complex 5 · the same entry in another collection · chain A against A, TM-score 1.00

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