P34896: Serine hydroxymethyltransferase, cytosolic (SHMT1)

Serine hydroxymethyltransferase, cytosolic (SHMT1) is a 483-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P34896.

Gene
SHMT1
Organism
Homo sapiens
Length
483 residues
Mean pLDDT
96.6
Model
AF-P34896-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 96.6 (very high overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate95%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Pyridoxal phosphate (PLP)-dependent enzyme that catalyzes the reversible conversion of serine and tetrahydrofolate (THF) to glycine and 5,10-methylene THF, serving as a critical component of the folate cycle and facilitating one-carbon biosynthetic reactions essential for methionine, purine, and pyrimidine synthesis (PubMed:24698160, PubMed:30035852, PubMed:38996576). While its central activity involves serine cleavage, the detailed catalytic mechanisms remain under study, including both retro-aldol cleavage of the PLP-serine C(alpha)-C(beta) bond followed by formaldehyde condensation with THF, and alternative nucleophilic displacement mechanisms of the C(alpha) atom of PLP-serine aldimine…

Subunit structure

Homotetramer comprising two obligate dimers (PubMed:24698160, PubMed:25619277, PubMed:30035852, PubMed:38996576, PubMed:9753690). Identified in complex with ABRAXAS2 and the other subunits of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (PubMed:24075985). Part of the de novo thymidylate synthesis complex composed at least by SHMT1, DHFR and TYMS…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
7RJPX-ray1.25 ÅB=270-275
7RJLX-ray1.5 ÅC/D=270-275
1BJ4X-ray2.65 ÅA=11-480
6M5WX-ray3.1 ÅA=1-483
8R7HEM3.29 ÅA/B/C/D=1-483
8XNDX-ray3.45 ÅA/B/C/D=11-480
8A11EM3.52 ÅA/B/C/D=1-483
6FL5X-ray3.6 ÅA/D/G/J=11-481

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