MolNFT v1 · #29770 · protein

Catalytic domain of human calpain-9

1ZIV · Calpain 9: “Catalytic domain of human calpain-9”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.43). MolNFT v1 #29770 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1ZIV
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calpain 9
EC: 3.4.22.-
UniProt: O14815
Ligands: CA
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calpain 9 (EC 3.4.22.-)	protein	308	31% helix, 21% strand	O14815

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
BME · Beta-mercaptoethanol · additive · 2 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.43	0.78	15	empty

Modifications

Observed in the structure: 2 covalent (additive adduct).

Compared structures

1ZIV · Catalytic Domain of Human Calpain-9 · the same entry in another collection · chain A against A, TM-score 1.00
O14815 · AlphaFold monomer V2.0 prediction for calpain-9 (O14815) · a predicted model of the same protein · chain A against A, TM-score 0.64

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 O14815
Elsewhere: RCSB PDB 1ZIV · PDBe 1ZIV · UniProt O14815

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