6M5W: Serine hydroxymethyltransferase, cytosolic

Co-crystal structure of human serine hydroxymethyltransferase 1 in complex with Pyridoxal 5'-phosphate (PLP) and glycodeoxycholic acid. Determined by X-ray diffraction at 3.1 Å resolution. Released 20 Jan 2021.

Method
X-ray diffraction
Resolution
3.1 Å
Organism
Homo sapiens
Chains
1
Atoms
3,662
Mol. weight
56.04 kDa
Ligands
GLY, DXC, PLP
Released
20 Jan 2021

Explore 6M5W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6M5W contains 25 α-helices and 24 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: 25 helices, 24 β-strands

ElementResiduesLengthSheet
α-helix15-239
α-helix26-294
α-helix31-4515
β-strand48-4921
β-strand5112
α-helix59-657
α-helix68-703
β-strand76-7723
β-strand80-8123
α-helix88-10316
β-strand111-11444
α-helix120-13112
β-strand137-13934
β-strand14115
α-helix149-1513
β-strand15416
β-strand15916
α-helix162-1665
β-strand168-16924
β-strand17215
β-strand17417
β-strand18117
α-helix183-19311
β-strand197-20154
α-helix211-22111
β-strand224-22854
α-helix229-2313
α-helix233-2386
α-helix244-2463
β-strand250-25454
α-helix257-2593
β-strand265-27064
β-strand272-27328
β-strand285-28628
α-helix288-2947
α-helix295-3006
α-helix306-31914
α-helix322-34423
β-strand348-34922
β-strand358-36252
α-helix363-3653
α-helix370-37910
β-strand382-38321
β-strand385-38732
β-strand400-40452
α-helix406-4094
α-helix415-43925
α-helix445-4539
α-helix455-47218

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine hydroxymethyltransferase, cytosolicAprotein503Homo sapiensP34896 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6M5W_1 Serine hydroxymethyltransferase, cytosolic (chains A)
MGSSHHHHHHSSGLVPRGSHMTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKE
SNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA
LQAYKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKI
SATSIFFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADE
NGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKT
GKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSE
ALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSG
LRLGTPALTSRGLLEKDFQKVAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAA
VQALREEVESFASLFPLPGLPDF

Ligands and cofactors

IDNameFormulaCopies
GLYGlycineC2 H5 N O21
DXC(3ALPHA,5BETA,12ALPHA)-3,12-dihydroxycholan-24-oic acidC24 H40 O41
PLPPyridoxal-5'-phosphateC8 H10 N O6 P1

Primary citation

Structural basis for selective inhibition of human serine hydroxymethyltransferase by secondary bile acid conjugate. Ota, T., Senoo, A., Shirakawa, M. et al. iScience (2021) 24:102036-102036. DOI 10.1016/j.isci.2021.102036 · PubMed

Other PDB entries of the same protein (UniProt P34896 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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