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X-ray crystal structure of a serine hydroxymethyl transferase in apo form from burkholderia cenocepacia

Analyse X-ray crystal structure of a serine hydroxymethyl transferase in apo form from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MSO
Type
protein
Length
765 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serine hydroxymethyltransferase
EC
2.1.2.1
UniProt
B4ECY9
Ligands
PO4
Pockets
6 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerine hydroxymethyltransferase (EC 2.1.2.1)protein38351% helix, 14% strandB4ECY9
BSerine hydroxymethyltransferase (EC 2.1.2.1)protein38251% helix, 14% strandB4ECY9

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 3 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15300.620.7569PO4
22730.590.7940empty
33580.580.7652PO4
41210.470.7915empty
51210.380.7415empty

Interfaces

1 interface between chains.

  • A–B · 3105 Ų buried · 46 hydrogen bonds · protein-protein

Compared structures

  • 4MSO · X-ray crystal structure of a serine hydroxymethyl transferase in apo form from… · the same entry in another collection · chain A against A, TM-score 1.00

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