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Structure and function study of rice bifunctional alpha- AMYLASE/SUBTILISIN inhibitor from oryza sativa

Analyse Structure and function study of rice bifunctional alpha- AMYLASE/SUBTILISIN… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QN4
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-AMYLASE/SUBTILISIN inhibitor
UniProt: P29421
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alpha-AMYLASE/SUBTILISIN inhibitor	protein	159	2% helix, 43% strand	P29421

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	348	0.57	0.76	40	empty

Interfaces

1 interface between chains.

A–B · 479 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2QN4 · Structure and function study of rice bifunctional alpha-amylase/subtilisin inhibitor from… · the same entry in another collection · chain A against A, TM-score 1.00
P29421 · AlphaFold monomer V2.0 prediction for alpha-AMYLASE/SUBTILISIN inhibitor (P29421) · 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 P29421
Elsewhere: RCSB PDB 2QN4 · PDBe 2QN4 · UniProt P29421

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