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Crystal structure of maltose transacetylase from geobacillus kaustophilus

Analyse Crystal structure of maltose transacetylase from geobacillus kaustophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IC7
Type: protein
Length: 555 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltose transacetylase
EC: 2.3.1.79
UniProt: Q75TD0
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Maltose transacetylase (EC 2.3.1.79)	protein	185	22% helix, 30% strand	Q75TD0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	87	0.76	0.99	23	empty
2	486	0.76	0.84	46	empty
3	639	0.75	0.81	65	empty
4	653	0.73	0.79	64	empty
5	596	0.72	0.80	60	empty

Interfaces

3 interfaces between chains.

A–B · 1320 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1254 Å² buried · 17 hydrogen bonds · protein-protein
A–C · 1241 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

2IC7 · Crystal Structure of Maltose Transacetylase from Geobacillus kaustophilus · 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 Q75TD0
Elsewhere: RCSB PDB 2IC7 · PDBe 2IC7 · UniProt Q75TD0

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