8SSJ: Serine hydroxymethyltransferase, mitochondrial

Room-temperature X-ray structure of human mitochondrial serine hydroxymethyltransferase (hSHMT2). Determined by X-ray diffraction at 2.5 Å resolution. Released 16 Aug 2023.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
2
Atoms
7,454
Mol. weight
104.36 kDa
Released
16 Aug 2023

Explore 8SSJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SSJ contains 50 α-helices and 44 β-strands across 2 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: 25 helices, 23 β-strands

ElementResiduesLengthSheet
α-helix49-524
α-helix54-6916
β-strand71-7221
α-helix82-887
α-helix91-944
β-strand99-10022
β-strand103-10422
α-helix110-12617
β-strand134-13743
α-helix143-15412
β-strand160-16453
α-helix172-1743
β-strand17714
β-strand18214
α-helix185-1873
β-strand191-19553
β-strand197-19825
β-strand203-20425
α-helix206-21611
β-strand220-22343
α-helix234-24411
β-strand247-25153
α-helix256-2605
α-helix267-2693
β-strand273-27753
α-helix280-2823
β-strand288-29363
β-strand29616
α-helix3071
β-strand30816
α-helix3091
α-helix312-3176
α-helix318-3236
α-helix329-34113
α-helix345-36723
β-strand371-37227
α-helix373-3753
β-strand381-38557
α-helix393-4019
β-strand405-40621
β-strand408-41037
β-strand41318
β-strand41518
β-strand423-42757
α-helix429-4335
α-helix438-46124
α-helix465-47410
α-helix476-49419
Chain B: 25 helices, 21 β-strands
ElementResiduesLengthSheet
α-helix49-524
α-helix54-6916
β-strand71-7229
α-helix82-887
α-helix91-944
β-strand99-100210
β-strand103-104210
α-helix110-12617
β-strand134-137411
α-helix143-15412
β-strand160-164511
α-helix166-1683
α-helix172-1743
β-strand177112
β-strand182112
α-helix185-1873
β-strand191-195511
β-strand197113
β-strand204113
α-helix206-21611
β-strand220-223411
α-helix234-24411
β-strand247-251511
α-helix256-2605
α-helix267-2693
β-strand273-277511
α-helix280-2823
β-strand288-293611
β-strand296114
β-strand308114
α-helix311-3177
α-helix318-3236
α-helix329-34113
α-helix345-36622
β-strand371-372215
α-helix373-3753
β-strand381-385515
α-helix387-3893
α-helix393-4019
β-strand405-40629
β-strand408-410315
β-strand423-427515
α-helix429-4335
α-helix438-45922
α-helix465-47410
α-helix476-49419

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine hydroxymethyltransferase, mitochondrialA, Bprotein468Homo sapiensP34897 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>8SSJ_1 Serine hydroxymethyltransferase, mitochondrial (chains A, B)
GEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKY
SEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQ
PHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLIDYNQLALTARLF
RPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTT
TTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVA
VALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARA
ERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGL
EVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH

Primary citation

Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography. Drago, V.N., Campos, C., Hooper, M. et al. Commun Chem (2023) 6:162-162. DOI 10.1038/s42004-023-00964-9 · PubMed

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

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