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Thermus maltogenic amylase in complex with beta-CD

Analyse Thermus maltogenic amylase in complex with beta-CD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GVI
Type: protein
Length: 1,176 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltogenic amylase
UniProt: O69007
Ligands: GLC
Pockets: 12 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Maltogenic amylase	protein	588	27% helix, 24% strand	O69007

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 14 copies · chains B, A

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

Pockets

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1065	0.87	0.88	133	empty
2	859	0.86	0.88	92	empty
3	368	0.67	0.80	31	GLC
4	328	0.67	0.81	33	GLC
5	193	0.67	0.86	28	empty

Interfaces

1 interface between chains.

A–B · 2932 Å² buried · 46 hydrogen bonds · protein-protein

Compared structures

1GVI · Thermus maltogenic amylase in complex with beta-CD · 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 O69007
Elsewhere: RCSB PDB 1GVI · PDBe 1GVI · UniProt O69007

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