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Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis, ligand-free form

Analyse Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZXG
Type
protein
Length
879 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cyclic maltosyl-maltose hydrolase
UniProt
D2YYE1
Ligands
CA
Pockets
4 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACyclic maltosyl-maltose hydrolaseprotein44036% helix, 20% strandD2YYE1
BCyclic maltosyl-maltose hydrolaseprotein43937% helix, 21% strandD2YYE1

Ligands and binding sites

  • CA · Calcium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14050.820.9043empty
2580.570.9014empty
31480.430.7520empty
41400.420.7523empty

Interfaces

1 interface between chains.

  • A–B · 1140 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 5ZXG · Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from Arthrobacter globiformis… · the same entry in another collection · chain A against A, TM-score 1.00

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