2WVN: HET-s N-terminal domain

Structure of the HET-s N-terminal domain. Determined by X-ray diffraction at 2.62 Å resolution. Released 28 Jul 2010.

Method: X-ray diffraction
Resolution: 2.62 Å
Organism: PODOSPORA ANSERINA
Chains: 1
Atoms: 1,694
Mol. weight: 25.53 kDa
Released: 28 Jul 2010

Explore 2WVN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WVN contains 16 α-helices and 4 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: 16 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	14-24	11
α-helix	25-27	3
β-strand	28-30	3	1
β-strand	31	1	2
α-helix	32-37	6
α-helix	38-58	21
α-helix	65-68	4
α-helix	75-101	27
α-helix	107-110	4
α-helix	111	1
β-strand	112	1	2
α-helix	113	1
α-helix	115-117	3
α-helix	120-136	17
α-helix	142-144	3
β-strand	148-150	3	1
α-helix	153-172	20
α-helix	177-186	10
α-helix	194-203	10
α-helix	209-222	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Small S protein	A	protein	229	PODOSPORA ANSERINA	Q03689 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2WVN_1 SMALL S PROTEIN (chains A)
GSMSEPFGIVAGALNVAGLFNNCVDCFEYVQLGRPFGRDYERCQLRLDIAKARLSRWGEA
VKINDDPRFHSDAPTDKSVQLAKSIVEEILLLFESAQKTSKRYELVADQQDLVVFEDKDM
KPIGRALHRRLNDLVSRRQKQTSLAKKTAWALYDGKSLEKIVDQVARFVDELEKAFPIEA
VCHKLAEIEIEEVEDEASLTILKDAAGGIDAAMSDAAAQKIDAIVGRNS

Primary citation

The Mechanism of Prion Inhibition by Het-S. Greenwald, J., Buhtz, C., Ritter, C. et al. Mol Cell (2010) 38:889. DOI 10.1016/J.MOLCEL.2010.05.019 · PubMed

Other PDB entries of the same protein (UniProt Q03689 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2WVQ 2.0 Å, Structure of the HET-s N-terminal domain. Mutant D23A, P33H
2KJ3 High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by…
2LBU HADDOCK calculated model of Congo red bound to the HET-s amyloid
2MUS HADDOCK calculated model of LIN5001 bound to the HET-s amyloid
2RNM Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

Browse structure collections

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