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Crystal structure of H307A mutant of thermotoga maritima TMPEP1050 aminopeptidase

Analyse Crystal structure of H307A mutant of thermotoga maritima TMPEP1050… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NE8
Type
protein
Length
617 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aminopeptidase
EC
3.4.11.1
UniProt
Q9X0E0
Pockets
2 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAminopeptidase (EC 3.4.11.1)protein30927% helix, 31% strandQ9X0E0
BAminopeptidase (EC 3.4.11.1)protein30828% helix, 31% strandQ9X0E0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14070.620.7766empty
2520.250.7312empty

Interfaces

1 interface between chains.

  • A–B · 551 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 5NE8 · Crystal structure of H307A mutant of Thermotoga maritima TmPEP1050 aminopeptidase · the same entry in another collection · chain A against A, TM-score 1.00

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