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NMR solution structure of the two domain ppiase slpa from escherichia COLI

Analyse NMR solution structure of the two domain ppiase slpa from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2M2A
Type
protein
Length
148 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fkbp-type 16 kda peptidyl-prolyl cis-trans isomerase
EC
5.2.1.8
UniProt
P0AEM0
Pockets
1 · best druggability 0.46

Structure

solution nmr · 1 distinct chain · 11% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFkbp-type 16 kda peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)protein14811% helix, 34% strandP0AEM0

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11590.460.7533empty

Compared structures

  • 2M2A · NMR solution structure of the two domain PPIase SlpA from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
  • P0AEM0 · AlphaFold monomer V2.0 prediction for fkbp-type 16 kda peptidyl- prolyl cis-trans… · a predicted model of the same protein · chain A against A, TM-score 0.79

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