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Solution structure of ZMP1, a zinc-dependent metalloprotease secreted by clostridium difficile

Analyse Solution structure of ZMP1, a zinc-dependent metalloprotease secreted by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N6J
Type: protein
Length: 195 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Zinc metalloprotease ZMP1
EC: 3.4.24.-
UniProt: Q183R7
Ligands: ZN
Pockets: 1 · best druggability 0.57

Structure

solution nmr · 1 distinct chain · 54% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zinc metalloprotease ZMP1 (EC 3.4.24.-)	protein	195	54% helix, 6% strand	Q183R7

Ligands and binding sites

ZN · Zinc ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	242	0.57	0.78	24	empty

Compared structures

2N6J · Solution structure of Zmp1, a zinc-dependent metalloprotease secreted by Clostridium… · the same entry in another collection · chain A against A, TM-score 1.00
Q183R7 · AlphaFold monomer V2.0 prediction for pro-pro endopeptidase (Q183R7) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q183R7
Elsewhere: RCSB PDB 2N6J · PDBe 2N6J · UniProt Q183R7

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