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Crystal structure of aminopeptidase

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

PDB
2IJZ
Type
protein
Length
4,548 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable M18-family aminopeptidase 2
EC
3.4.11.-
UniProt
Q9HYZ3
Pockets
20 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LProbable M18-family aminopeptidase 2 (EC 3.4.11.-)protein37914% helix, 18% strandQ9HYZ3

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19290.830.8481empty
27560.830.8671empty
38900.820.84137empty
49970.810.8380empty
510770.810.8282empty

Interfaces

18 interfaces between chains.

  • A–D · 3180 Ų buried · 36 hydrogen bonds · protein-protein
  • I–L · 3170 Ų buried · 33 hydrogen bonds · protein-protein
  • G–J · 3163 Ų buried · 33 hydrogen bonds · protein-protein
  • E–H · 3155 Ų buried · 35 hydrogen bonds · protein-protein
  • C–F · 3147 Ų buried · 38 hydrogen bonds · protein-protein

Compared structures

  • 2IJZ · Crystal structure of aminopeptidase · the same entry in another collection · chain L against L, TM-score 1.00

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