Research workbench

Crystal structure of aspartic proteinase from irpex lacteus

Analyse Crystal structure of aspartic proteinase from irpex lacteus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WKR
Type: protein
Length: 345 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polyporopepsin; Pepstatin
EC: 3.4.23.29
UniProt: P17576
Ligands: IVA, SO4

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polyporopepsin (EC 3.4.23.29)	protein	340	14% helix, 43% strand	P17576
I	Pepstatin	protein	5	0% helix, 20% strand	—

Ligands and binding sites

IVA · Isovaleric acid · ligand · chains A, I
SO4 · Sulfate ion · ion · 7 copies · chains A

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

Interfaces

1 interface between chains.

A–I · 551 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified, 1 covalent (nonstandard, covalent ligand).

Compared structures

1WKR · Crystal structure of aspartic proteinase from Irpex lacteus · the same entry in another collection · chain A against A, TM-score 1.00
P17576 · AlphaFold monomer V2.0 prediction for polyporopepsin (P17576) · 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 P17576
Elsewhere: RCSB PDB 1WKR · PDBe 1WKR · UniProt P17576

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