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Crystal structure of a methionine aminopeptidase from mycobacterium abscessus

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

PDB
3TAV
Type
protein
Length
528 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methionine aminopeptidase
EC
3.4.11.18
UniProt
B1MGB2
Ligands
MLT, LMR, MG, NA, CL
Pockets
5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMethionine aminopeptidase (EC 3.4.11.18)protein26430% helix, 26% strandB1MGB2

Ligands and binding sites

  • MLT · D-malate · ligand · chains A
  • LMR · (2S)-2-hydroxybutanedioic acid · ligand · chains A
  • MG · Magnesium ion · metal · 4 copies · chains A, B
  • NA · Sodium ion · metal · 2 copies · chains A, B
  • CL · Chloride ion · ion · 3 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110050.790.8094empty
21320.560.8224CL
31370.550.8122LMR
4570.420.8218empty
5510.400.8217empty

Interfaces

1 interface between chains.

  • A–B · 485 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 3TAV · Crystal structure of a Methionine Aminopeptidase from Mycobacterium abscessus · the same entry in another collection · chain B against B, TM-score 1.00

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