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The crystal structure of novel exo-type maltose-forming AMYLASE(PY04_0872) from pyrococcus sp. ST04

Analyse The crystal structure of novel exo-type maltose-forming AMYLASE(PY04_0872) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CMR
Type
protein
Length
1,192 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycosyl HYDROLASE/DEACETYLASE family protein
UniProt
I3RE04
Pockets
6 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycosyl HYDROLASE/DEACETYLASE family proteinprotein59750% helix, 15% strandI3RE04
BGlycosyl HYDROLASE/DEACETYLASE family proteinprotein59549% helix, 16% strandI3RE04

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14410.760.8538empty
24500.750.8440empty
37760.750.7977empty
4520.690.9819empty
51180.380.7423empty

Interfaces

1 interface between chains.

  • A–B · 1145 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 34 modified, 2 disulfide (engineered, disulfide).

Compared structures

  • 4CMR · The crystal structure of novel exo-type maltose-forming amylase(Py04_0872) from… · the same entry in another collection · chain A against A, TM-score 1.00

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