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Crystal structure of an alpha-amylase from lactobacillus plantarum

Analyse Crystal structure of an alpha-amylase from lactobacillus plantarum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DHU
Type: protein
Length: 1,680 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-amylase
EC: 3.2.1.1
UniProt: Q88ZW5
Pockets: 18 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Alpha-amylase (EC 3.2.1.1)	protein	422	36% helix, 21% strand	Q88ZW5
B, D	Alpha-amylase (EC 3.2.1.1)	protein	418	36% helix, 21% strand	Q88ZW5

Pockets

18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	210	0.80	0.94	37	empty
2	897	0.77	0.80	94	empty
3	62	0.67	0.95	25	empty
4	50	0.62	0.94	23	empty
5	230	0.57	0.78	25	empty

Interfaces

4 interfaces between chains.

B–C · 872 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 859 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 375 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 242 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3DHU · Crystal structure of an alpha-amylase from Lactobacillus plantarum · the same entry in another collection · chain B against B, 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 Q88ZW5
Elsewhere: RCSB PDB 3DHU · PDBe 3DHU · UniProt Q88ZW5

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