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Crystal structure of acutolysin-C, a hemorrhagic toxin from the snake venom of agkistrodon acutus, at 2.2 a resolution

Analyse Crystal structure of acutolysin-C, a hemorrhagic toxin from the snake venom of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QUA
Type: protein
Length: 197 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acutolysin-C
UniProt: Q9W7S2
Ligands: ZN
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acutolysin-C	protein	197	40% helix, 17% strand	Q9W7S2

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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	115	0.50	0.80	25	ZN

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1QUA · Crystal structure of acutolysin-C, a hemorrhagic toxin from the snake venom of… · the same entry in another collection · chain A against A, TM-score 1.00
Q9W7S2 · AlphaFold monomer V2.0 prediction for snake venom metalloproteinase aculysin-1 (Q9W7S2) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9W7S2
Elsewhere: RCSB PDB 1QUA · PDBe 1QUA · UniProt Q9W7S2

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