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NMR structure of E. COLI trigger factor in complex with unfolded PHOA220-310

Analyse NMR structure of E. COLI trigger factor in complex with unfolded PHOA220-310 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2MLX
Type
protein
Length
523 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trigger factor; Alkaline phosphatase
EC
5.2.1.8
UniProt
U6N325, U6N3P1
Pockets
6 · best druggability 0.77

Structure

solution nmr · 2 distinct chains · 40% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATrigger factor (EC 5.2.1.8)protein43247% helix, 22% strandU6N325
BAlkaline phosphataseprotein918% helix, 0% strandU6N3P1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11280.770.9520empty
25440.630.7553empty
31240.620.8523empty
4930.370.7616empty
5610.350.7715empty

Interfaces

1 interface between chains.

  • A–B · 3136 Ų buried · 73 hydrogen bonds · protein-protein

Compared structures

  • 2MLX · NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310 · the same entry in another collection · chain A against A, TM-score 1.00

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