GL1X · GenesisL1 explorer

Research workbench

Human calmodulin bound to a peptide of human NADPH oxidase 5

Analyse Human calmodulin bound to a peptide of human NADPH oxidase 5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SZ5
Type
protein
Length
165 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P0DP24, Q96PH1
Ligands
CA

Structure

x-ray diffraction · 3 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein144—P0DP24
B—protein11—Q96PH1
C—protein10—Q96PH1

Ligands and binding sites

  • CA · Calcium ion · metal · 4 copies · chains A

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

Compared structures

  • 6SZ5 · Human calmodulin bound to a peptide of human NADPH oxidase 5 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96PH1 · AlphaFold monomer V2.0 prediction for NADPH oxidase 5 (Q96PH1) · a predicted model of the same protein · chain C against A, TM-score 0.85
  • P0DP24 · AlphaFold monomer V2.0 prediction for calmodulin-2 (P0DP24) · a predicted model of the same protein · chain A against A, TM-score 0.84

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.