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MolNFT v1 · #20968 · protein

E75Q mutant of rabbit cytosolic serine hydroxymethyltransferase

1RVU · Serine hydroxymethyltransferase, cytosolic: “E75Q mutant of rabbit cytosolic serine hydroxymethyltransferase”. X-ray diffraction, 2 ligands (PLP, PO4), 11 pockets (best druggability 0.77). MolNFT v1 #20968 on GenesisL1: 3D…

PDB
1RVU
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
11 · 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 · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.770.9828empty
23630.740.8641PLP
33680.730.8443PO4, PLP
4560.710.9828empty
52160.520.7630empty

Interfaces

1 interface between chains.

  • A–B · 4630 Ų buried · 59 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 1RVU · E75Q 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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