Research workbench

Crystal structure of acylphosphatase from pyrococcus horikoshii

Analyse Crystal structure of acylphosphatase from pyrococcus horikoshii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V3Z
Type: protein
Length: 180 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acylphosphatase
EC: 3.6.1.7
UniProt: P84142
Ligands: K, CL
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acylphosphatase (EC 3.6.1.7)	protein	90	24% helix, 42% strand	P84142

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B

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	0.36	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 702 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1V3Z · Crystal Structure of Acylphosphatase from Pyrococcus horikoshii · the same entry in another collection · chain A against A, TM-score 1.00
P84142 · AlphaFold monomer V2.0 prediction for acylphosphatase (P84142) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P84142
Elsewhere: RCSB PDB 1V3Z · PDBe 1V3Z · UniProt P84142

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.