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Structure of maize BZR1-type beta-amylase provides new insights into its noncatalytic adaptation

Analyse Structure of maize BZR1-type beta-amylase provides new insights into its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7UPV
Type: protein
Length: 440 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.84
Source: Zea mays
Molecule: Beta-amylase
EC: 3.2.1.2
UniProt: A0A1D6QTZ9
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · resolution 1.84 · 1 distinct chain · 40% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-amylase (EC 3.2.1.2)	protein	440	40% helix, 14% strand	A0A1D6QTZ9

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.76	0.99	17	empty
2	617	0.74	0.81	61	empty
3	105	0.42	0.77	17	empty
4	81	0.34	0.75	13	empty
5	62	0.27	0.73	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7UPV · Structure of maize BZR1-type beta-amylase provides new insights into its noncatalytic… · the same entry in another collection · 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 A0A1D6QTZ9
Elsewhere: RCSB PDB 7UPV · PDBe 7UPV · UniProt A0A1D6QTZ9

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