Research workbench

Structure and refinement at 1.8 ångströms resolution of the aspartic proteinase from rhizopus chinensis

Analyse Structure and refinement at 1.8 ångströms resolution of the aspartic proteinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2APR
Type: protein
Length: 325 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rhizopuspepsin
EC: 3.4.23.6
UniProt: P06026
Ligands: CA
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rhizopuspepsin (EC 3.4.23.6)	protein	325	14% helix, 46% strand	P06026

Ligands and binding sites

CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	337	0.59	0.77	43	CA
2	50	0.33	0.78	13	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2APR · Structure and refinement at 1.8 ångströms resolution of the aspartic proteinase from… · the same entry in another collection · chain A against A, TM-score 1.00
P06026 · AlphaFold monomer V2.0 prediction for rhizopuspepsin (P06026) · a predicted model of the same protein · 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
Every structure of UniProt P06026
Elsewhere: RCSB PDB 2APR · PDBe 2APR · UniProt P06026

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