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E75L mutant of rabbit cytosolic serine hydroxymethyltransferase

Analyse E75L mutant of rabbit cytosolic serine hydroxymethyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1RV4
Type
protein
Length
929 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serine hydroxymethyltransferase, cytosolic
EC
2.1.2.1
UniProt
P07511
Ligands
PLP, PO4
Pockets
10 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerine hydroxymethyltransferase, cytosolic (EC 2.1.2.1)protein46350% helix, 14% strandP07511
BSerine hydroxymethyltransferase, cytosolic (EC 2.1.2.1)protein46650% helix, 14% strandP07511

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
  • PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1910.770.9829empty
23690.740.8546PO4, PLP
33730.720.8350PO4, PLP
42300.520.7627empty
51600.490.7830empty

Interfaces

1 interface between chains.

  • A–B · 4672 Ų buried · 50 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).

Compared structures

  • 1RV4 · E75L mutant of rabbit cytosolic serine hydroxymethyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
  • P07511 · AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase, cytosolic (P07511) · a predicted model of the same protein · chain B against A, TM-score 1.00

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