2WVQ: HET-s N-terminal domain. Mutant D23A, P33H

Structure of the HET-s N-terminal domain. Mutant D23A, P33H. Determined by X-ray diffraction at 2.0 Å resolution. Released 28 Jul 2010.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: PODOSPORA ANSERINA
Chains: 2
Atoms: 3,577
Mol. weight: 51.22 kDa
Ligands: DTU, DTT
Released: 28 Jul 2010

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

Secondary structure: helices and β-sheets

2WVQ contains 26 α-helices and 8 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: 14 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	75-104	30
α-helix	107-110	4
β-strand	112	1	2
α-helix	115-117	3
α-helix	120-136	17
α-helix	143-147	5
β-strand	148-150	3	1
α-helix	153-172	20
α-helix	177-187	11
α-helix	194-203	10
α-helix	209-220	12

Chain B: 12 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	14-24	11
β-strand	28-30	3	3
β-strand	31	1	4
α-helix	32-37	6
α-helix	38-59	22
α-helix	65-68	4
α-helix	75-104	30
α-helix	107-109	3
β-strand	112	1	4
α-helix	115-117	3
α-helix	120-134	15
β-strand	148-150	3	3
α-helix	153-172	20
α-helix	177-187	11
α-helix	194-203	10
α-helix	209-220	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Small S protein	A, B	protein	225	PODOSPORA ANSERINA	Q03689 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2WVQ_1 SMALL S PROTEIN (chains A, B)
MRGSHHHHHHLVPRGSNVAGLFNNCVACFEYVQLGRHFGRDYERCQLRLDIAKARLSRWG
EAVKINDDPRFHSDAPTDKSVQLAKSIVEEILLLFESAQKTSKRYELVADQQDLVVFEDK
DMKPIGRALHRRLNDLVSRRQKQTSLAKKTAWALYDGKSLEKIVDQVARFVDELEKAFPI
EAVCHKLAEIEIEEVEDEASLTILKDAAGGIDAAMSDAAAQKIDA

Ligands and cofactors

ID	Name	Formula	Copies
DTU	(2R,3S)-1,4-dimercaptobutane-2,3-diol	C4 H10 O2 S2	1
DTT	2,3-dihydroxy-1,4-dithiobutane	C4 H10 O2 S2	1

Primary citation

The mechanism of prion inhibition by HET-S. Greenwald, J., Buhtz, C., Ritter, C. et al. Mol Cell (2010) 38:889-899. 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:

2WVN 2.62 Å, Structure of the HET-s N-terminal domain
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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