32JA: PDB entry 32JA

Name: PDB 32JA: Structure of the pathogenic variant T186R of Human SHMT2 in the apo open dimeric conformation
Published: 2026-09-02
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Structure of the pathogenic variant T186R of Human SHMT2 in the apo open dimeric conformation. Determined by X-ray diffraction at 2.2 Å resolution. Released 2 Sept 2026.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,282
Mol. weight: 53.87 kDa
Released: 2 Sept 2026

Explore 32JA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

32JA contains 22 α-helices and 18 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 22 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	49-52	4
α-helix	54-69	16
β-strand	71-72	2	1
α-helix	82-88	7
α-helix	91-94	4
α-helix	111-126	16
β-strand	134-137	4	2
α-helix	143-154	12
β-strand	161-162	2	2
β-strand	164	1	3
β-strand	195	1	3
β-strand	197-198	2	4
β-strand	203-204	2	4
α-helix	206-216	11
β-strand	220-223	4	2
α-helix	234-244	11
β-strand	247-251	5	2
α-helix	256-260	5
α-helix	267-269	3
β-strand	273-277	5	2
β-strand	288-293	6	2
β-strand	296-299	4	5
β-strand	306-308	3	5
α-helix	309	1
α-helix	312-317	6
α-helix	318-323	6
α-helix	329-341	13
α-helix	345-367	23
β-strand	371-372	2	6
α-helix	373-375	3
β-strand	381-385	5	6
α-helix	387-389	3
α-helix	393-402	10
β-strand	405-406	2	1
β-strand	408-410	3	6
β-strand	423-427	5	6
α-helix	429-433	5
α-helix	438-460	23
α-helix	465-474	10
α-helix	476-493	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Isoform 3 of Serine hydroxymethyltransferase, mitochondrial	A	protein	486	Homo sapiens	P34897 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>32JA_1 Isoform 3 of Serine hydroxymethyltransferase, mitochondrial (chains A)
GSHMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASEN
FCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNV
QPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISARSIFFESMPYKLN
PKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGL
VAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFA
VFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTD
NHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFRE
DDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPM
PGFDEH

Primary citation

Structural and functional defects of mitochondrial serine hydroxymethyltransferase genetic variants responsible for a novel neurodevelopmental syndrome. Boumis, G., Breccia, S., Pistoia, G. et al. Front Chem Biol (2026) Volume 5 - 2026.

Other PDB entries of the same protein (UniProt P34897 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8AQL 1.23 Å, High-resolution crystal structure of human SHMT2
29LK 1.26 Å, High-resolution structure of human SHMT2 in complex with PLP-Ser (external aldimine)
9RWD 1.3 Å, High-resolution structure of human SHMT2 with covalently bound PLP (internal aldimine)
32JY 1.8 Å, Structure of the pathogenic variant G423S of Human SHMT2
6DK3 2.04 Å, Human mitochondrial serine hydroxymethyltransferase 2
9BOX 2.1 Å, Room-temperature X-ray structure of human mitochondrial serine hydroxymethyltransferase…
6QVL 2.28 Å, Human SHMT2 in complex with pemetrexed
6M5O 2.3 Å, Co-crystal structure of human serine hydroxymethyltransferase 2 in complex with…
6QVG 2.32 Å, Human SHMT2 in complex with lometrexol
8GKW 2.38 Å, Human mitochondrial serine hydroxymethyltransferase (SHMT2) in complex with PLP, glycine…
5V7I 2.47 Å, Crystal structure of homo sapiens serine hydroxymethyltransferase 2 (mitochondrial)…
8FJT 2.47 Å, Human mitochondrial serine hydroxymethyltransferase (SHMT2) in complex with PLP, glycine…

Browse structure collections

About this viewer

MolViewer shows 32JA directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.