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Alpha-amylase B in complex with maltotetraose and alpha-cyclodextrin

Analyse Alpha-amylase B in complex with maltotetraose and alpha-cyclodextrin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BCD
Type: protein
Length: 585 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha amylase, catalytic region
EC: 3.2.1.1
UniProt: Q2ADF2
Ligands: GLC, BGC, CA, NA
Pockets: 5 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha amylase, catalytic region (EC 3.2.1.1)	protein	585	25% helix, 29% strand	Q2ADF2

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 13 copies · chains A
BGC · beta-D-glucopyranose · sugar · chains A
CA · Calcium ion · metal · 7 copies · chains A
NA · Sodium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	171	0.53	0.79	24	empty
2	165	0.49	0.77	25	GLC
3	192	0.46	0.75	36	empty
4	98	0.40	0.77	21	empty
5	52	0.29	0.76	14	empty

Compared structures

3BCD · Alpha-amylase B in complex with maltotetraose and alpha-cyclodextrin · 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 Q2ADF2
Elsewhere: RCSB PDB 3BCD · PDBe 3BCD · UniProt Q2ADF2

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