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Crystal structure of the carica candamarcensis cysteine protease CMS1MS2 in complex with E-64.

Analyse Crystal structure of the carica candamarcensis cysteine protease CMS1MS2 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IOQ
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CMS1MS2
Ligands: E64, SO4
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CMS1MS2	protein	213	29% helix, 22% strand	—

Ligands and binding sites

E64 · N-[N-[1-hydroxycarboxyethyl-carbonyl]leucylamino-butyl]-guanidine · ligand · chains A
SO4 · Sulfate ion · ion · 8 copies · chains A
EDO · 1,2-ethanediol · additive · 10 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	53	0.30	0.75	17	SO4

Modifications

Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

3IOQ · Crystal structure of the Carica candamarcensis cysteine protease CMS1MS2 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 3IOQ · PDBe 3IOQ

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