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Crystal structure of protease-associated domain of arabidopsis VSR1 in complex with aleurain peptide

Analyse Crystal structure of protease-associated domain of arabidopsis VSR1 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TJX
Type: protein
Length: 156 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vacuolar-sorting receptor 1; Aleurain peptide
UniProt: P93026
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vacuolar-sorting receptor 1	protein	153	20% helix, 28% strand	P93026
B	Aleurain peptide	protein	3	0% helix, 0% strand	—

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	55	0.31	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 229 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4TJX · Crystal structure of protease-associated domain of Arabidopsis VSR1 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P93026 · AlphaFold monomer V2.0 prediction for vacuolar-sorting receptor 1 (P93026) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P93026
Elsewhere: RCSB PDB 4TJX · PDBe 4TJX · UniProt P93026

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