4H5I: Guanine Nucleotide Exchange Factor Sec12

Crystal Structure of the Guanine Nucleotide Exchange Factor Sec12 (P1 form). Determined by X-ray diffraction at 1.36 Å resolution. Released 7 Nov 2012.

Method
X-ray diffraction
Resolution
1.36 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
5,681
Mol. weight
80.62 kDa
Released
7 Nov 2012

Explore 4H5I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4H5I contains 8 α-helices and 56 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.

Chains A and B: 4 helices, 28 β-strands

ElementResiduesLengthSheet
β-strand5-951
β-strand14-2182
β-strand24-3072
β-strand40-4782
α-helix54-574
β-strand58-6582
α-helix71-733
β-strand75-7953
β-strand82-8653
α-helix91-966
β-strand103-10973
β-strand114-12183
β-strand133-13864
β-strand145-14954
β-strand155-16064
β-strand165-17174
β-strand178-18145
β-strand187-19155
β-strand196-20055
β-strand206-21055
β-strand217-226106
β-strand229-23686
β-strand242-25096
β-strand253-263116
β-strand269-27467
β-strand280-28567
β-strand290-29457
β-strand299-30467
β-strand312-31761
β-strand323-32861
β-strand332-33761
α-helix338-3392

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Guanine nucleotide-exchange factor SEC12A, Bprotein365Saccharomyces cerevisiaeP11655 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4H5I_1 Guanine nucleotide-exchange factor SEC12 (chains A, B)
MASMKFVTASYNVGYPAYGAKFLNNDTLLVAGGGGEGNNGIPNKLTVLRVDPTKDTEKEQ
FHILSEFALEDNDDSPTAIDASKGIILVGCNENSTKITQGKGNKHLRKFKYDKVNDQLEF
LTSVDFDASTNADDYTKLVYISREGTVAAIASSKVPAIMRIIDPSDLTEKFEIETRGEVK
DLHFSTDGKVVAYITGSSLEVISTVTGSCIARKTDFDKNWSLSKINFIADDTVLIAASLK
KGKGIVLTKISIKSGNTSVLRSKQVTNRFKGITSMDVDMKGELAVLASNDNSIALVKLKD
LSMSKIFKQAHSFAITEVTISPDSTYVASVSAANTIHIIKLPLNYANYTSMKQKISKLEH
HHHHH

Primary citation

The structure of sec12 implicates potassium ion coordination in sar1 activation. McMahon, C., Studer, S.M., Clendinen, C. et al. J Biol Chem (2012) 287:43599-43606. DOI 10.1074/jbc.M112.420141 · PubMed

Other PDB entries of the same protein (UniProt P11655 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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