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Catalytic domain of human calpain-1

Analyse Catalytic domain of human calpain-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ARY
Type: protein
Length: 644 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P07384

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	—	protein	322	—	P07384

Compared structures

2ARY · Catalytic domain of Human Calpain-1 · the same entry in another collection · chain A against A, TM-score 1.00
P07384 · AlphaFold monomer V2.0 prediction for calpain-1 catalytic subunit (P07384) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P07384
Elsewhere: RCSB PDB 2ARY · PDBe 2ARY · UniProt P07384

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