32JY: Pathogenic variant G423S of Human SHMT2

Name: PDB 32JY: Structure of the pathogenic variant G423S of Human SHMT2
Published: 2026-09-02
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Structure of the pathogenic variant G423S of Human SHMT2. Determined by X-ray diffraction at 1.8 Å resolution. Released 2 Sept 2026.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 14,842
Mol. weight: 216.57 kDa
Ligands: 1BO, PDO, BU1
Released: 2 Sept 2026

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

Secondary structure: helices and β-sheets

32JY contains 101 α-helices and 88 β-strands across 4 chains. 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: 26 helices, 21 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
β-strand	99-100	2	2
β-strand	103-104	2	2
α-helix	110-126	17
β-strand	134-137	4	3
α-helix	143-154	12
β-strand	160-164	5	3
α-helix	166-168	3
α-helix	172-174	3
β-strand	177	1	4
β-strand	182	1	4
α-helix	185-189	5
β-strand	191-195	5	3
β-strand	197	1	5
β-strand	204	1	5
α-helix	206-216	11
β-strand	220-223	4	3
α-helix	234-244	11
β-strand	247-251	5	3
α-helix	256-260	5
α-helix	267-269	3
β-strand	273-277	5	3
α-helix	280-282	3
β-strand	288-293	6	3
β-strand	296	1	6
α-helix	307	1
β-strand	308	1	6
α-helix	309	1
α-helix	311-317	7
α-helix	318-323	6
α-helix	329-341	13
α-helix	345-367	23
β-strand	371-372	2	7
α-helix	373-375	3
β-strand	381-385	5	7
α-helix	393-402	10
β-strand	405-406	2	1
β-strand	408-410	3	7
β-strand	423-427	5	7
α-helix	429-432	4
α-helix	438-459	22
α-helix	465-474	10
α-helix	476-494	19

Chain B: 26 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	49-52	4
α-helix	54-69	16
β-strand	71-72	2	8
α-helix	82-88	7
α-helix	91-94	4
β-strand	99-100	2	9
β-strand	103-104	2	9
α-helix	110-126	17
β-strand	134-137	4	10
α-helix	143-154	12
β-strand	160-162	3	10
β-strand	164	1	11
α-helix	166-168	3
α-helix	172-174	3
β-strand	177	1	12
β-strand	182	1	12
α-helix	185-189	5
β-strand	191-192	2	10
β-strand	195	1	11
β-strand	197	1	13
β-strand	204	1	13
α-helix	206-216	11
β-strand	220-223	4	10
α-helix	234-244	11
β-strand	247-251	5	10
α-helix	253-255	3
α-helix	256-261	6
α-helix	267-269	3
β-strand	273-277	5	10
α-helix	280-282	3
β-strand	288-293	6	10
β-strand	296	1	14
β-strand	308	1	14
α-helix	311-317	7
α-helix	318-323	6
α-helix	329-342	14
α-helix	345-367	23
β-strand	371-372	2	15
α-helix	373-375	3
β-strand	381-385	5	15
α-helix	387-389	3
α-helix	393-402	10
β-strand	405-406	2	8
β-strand	408-410	3	15
β-strand	423-427	5	15
α-helix	429-432	4
α-helix	438-459	22
α-helix	465-474	10
α-helix	476-493	18

Chain C: 25 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	49-52	4
α-helix	54-69	16
β-strand	71-72	2	16
α-helix	82-88	7
α-helix	91-94	4
β-strand	99-100	2	17
β-strand	103-104	2	17
α-helix	110-126	17
β-strand	134-137	4	18
α-helix	143-154	12
β-strand	160-162	3	18
β-strand	164	1	19
α-helix	166-168	3
α-helix	172-174	3
β-strand	177	1	20
β-strand	182	1	20
α-helix	185-189	5
β-strand	191-192	2	18
β-strand	195	1	19
β-strand	197	1	21
β-strand	204	1	21
α-helix	206-216	11
β-strand	220-223	4	18
α-helix	234-244	11
β-strand	247-251	5	18
α-helix	256-260	5
α-helix	267-269	3
β-strand	273-277	5	18
α-helix	280-282	3
β-strand	288-293	6	18
β-strand	296	1	22
β-strand	308	1	22
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	23
α-helix	373-375	3
β-strand	381-385	5	23
α-helix	387-389	3
α-helix	393-401	9
β-strand	405-406	2	16
β-strand	408-410	3	23
β-strand	423-427	5	23
α-helix	429-433	5
α-helix	438-459	22
α-helix	465-474	10
α-helix	476-494	19

Chain D: 24 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	49-52	4
α-helix	54-69	16
β-strand	71-72	2	24
α-helix	82-88	7
α-helix	91-94	4
β-strand	99-100	2	25
β-strand	103-104	2	25
α-helix	110-126	17
β-strand	134-137	4	26
α-helix	143-154	12
β-strand	160-164	5	26
α-helix	166-168	3
α-helix	172-174	3
β-strand	177	1	27
β-strand	182	1	27
α-helix	185-189	5
β-strand	191-195	5	26
β-strand	197	1	28
β-strand	204	1	28
α-helix	206-216	11
β-strand	220-223	4	26
α-helix	234-244	11
β-strand	247-251	5	26
α-helix	256-261	6
α-helix	267-269	3
β-strand	273-277	5	26
α-helix	280-282	3
β-strand	288-293	6	26
β-strand	296	1	29
β-strand	308	1	29
α-helix	312-317	6
α-helix	318-323	6
α-helix	329-342	14
α-helix	345-367	23
β-strand	371-372	2	30
α-helix	373-375	3
β-strand	381-385	5	30
α-helix	393-402	10
β-strand	405-406	2	24
β-strand	408-409	2	30
β-strand	423-427	5	30
α-helix	429-432	4
α-helix	438-460	23
α-helix	465-474	10
α-helix	476-493	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine hydroxymethyltransferase, mitochondrial	A, B, C, D	protein	486	Homo sapiens	P34897 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>32JY_1 Serine hydroxymethyltransferase, mitochondrial (chains A, B, C, D)
GSHMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASEN
FCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNV
QPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLN
PKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGL
VAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFA
VFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTD
NHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGSLRLGAPALTSRQFRE
DDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPM
PGFDEH

Ligands and cofactors

ID	Name	Formula	Copies
1BO	1-butanol	C4 H10 O	1
PDO	1,3-propandiol	C3 H8 O2	1
BU1	1,4-butanediol	C4 H10 O2	1

Water and common crystallization additives (EDO) are not listed.

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)
6DK3 2.04 Å, Human mitochondrial serine hydroxymethyltransferase 2
9BOX 2.1 Å, Room-temperature X-ray structure of human mitochondrial serine hydroxymethyltransferase…
32JA 2.2 Å, Structure of the pathogenic variant T186R of Human SHMT2 in the apo open dimeric…
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…

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