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Structure of wild type amidase at high temperature at 2.5 ångström resolution

Analyse Structure of wild type amidase at high temperature at 2.5 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5JZO
Type
protein
Length
1,686 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Intracellular PROTEASE/AMIDASE
EC
4.2.1.130
UniProt
A0A0H3AFW5
Pockets
15 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FIntracellular PROTEASE/AMIDASE (EC 4.2.1.130)protein28139% helix, 17% strandA0A0H3AFW5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18430.810.84105empty
21470.740.9239empty
37070.730.7970empty
44020.640.7853empty
51790.580.8126empty

Interfaces

10 interfaces between chains.

  • C–D · 1101 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 1089 Ų buried · 20 hydrogen bonds · protein-protein
  • E–F · 921 Ų buried · 18 hydrogen bonds · protein-protein
  • B–F · 480 Ų buried · 11 hydrogen bonds · protein-protein
  • C–F · 453 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 5JZO · Structure of wild type amidase at high temperature at 2.5 Angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00

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