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Human CARMA1 card domain

Analyse Human CARMA1 card domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4LWD
Type
protein
Length
90 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Caspase recruitment domain-containing protein 11
UniProt
Q9BXL7
Ligands
MG, SO4
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACaspase recruitment domain-containing protein 11protein9066% helix, 0% strandQ9BXL7

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A
  • SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1840.360.7614empty

Compared structures

  • 4LWD · Human CARMA1 CARD domain · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9BXL7 · AlphaFold monomer V2.0 prediction for caspase recruitment domain- containing protein 11… · a predicted model of the same protein · chain A against A, TM-score 0.91

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