2ZD7: VPS75

The structure of VPS75 (Vacuolar protein sorting-associated protein 75). Determined by X-ray diffraction at 1.85 Å resolution. Released 12 Aug 2008.

Method: X-ray diffraction
Resolution: 1.85 Å
Organisms: Saccharomyces cerevisiae, synthetic construct
Chains: 3
Atoms: 3,991
Mol. weight: 62.73 kDa
Released: 12 Aug 2008

Explore 2ZD7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ZD7 contains 24 α-helices and 12 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: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	7-51	45
α-helix	57-64	8
α-helix	68-71	4
α-helix	74-76	3
α-helix	77-80	4
β-strand	83-90	8	1
α-helix	91-93	3
β-strand	103-109	7	1
β-strand	112	1	2
β-strand	116	1	2
β-strand	119-128	10	1
β-strand	138-141	4	1
α-helix	150-155	6
α-helix	166-176	11
α-helix	179-182	4
α-helix	197-202	6
α-helix	203-208	6
α-helix	209-221	13

Chain B: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	12-51	40
α-helix	57-64	8
α-helix	68-71	4
α-helix	74-76	3
α-helix	77-80	4
β-strand	83-90	8	3
α-helix	91-93	3
β-strand	103-109	7	3
β-strand	112	1	4
β-strand	116	1	4
β-strand	119-128	10	3
β-strand	138-141	4	3
α-helix	150-152	3
α-helix	166-176	11
α-helix	179-182	4
α-helix	197-202	6
α-helix	203-208	6
α-helix	209-225	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vacuolar protein sorting-associated protein 75	A, B	protein	264	Saccharomyces cerevisiae	P53853 (AlphaFold model)
Evdlplsdeepss	C	protein	13	synthetic construct

Sequence of entity 1 (A, B), FASTA

>2ZD7_1 Vacuolar protein sorting-associated protein 75 (chains A, B)
MMSDQENENEHAKAFLGLAKCEEEVDAIEREVELYRLNKMKPVYEKRDAYIDEIAEFWKI
VLSQHVSFANYIRASDFKYIDTIDKIKVEWLALESEMYDTRDFSITFHFHGIEGDFKEQQ
VTKVFQIKKGKDDQEDGILTSEPVPIEWPQSYDSINPDLIKDKRSPEGKKKYRQGMKTIF
GWFRWTGLKPGKEFPHGDSLASLFSEEIYPFCVKYYAEAQRDLEDEEGESGLSADGDSED
DDGSLGEVDLPLSDEEPSSKKRKV

Sequence of entity 2 (C), FASTA

>2ZD7_2 EVDLPLSDEEPSS (chains C)
EVDLPLSDEEPSS

Primary citation

Histone chaperone specificity in Rtt109 activation. Park, Y.J., Sudhoff, K.B., Andrews, A.J. et al. Nat Struct Mol Biol (2008) 15:957-964. DOI 10.1038/nsmb.1480 · PubMed

Other PDB entries of the same protein (UniProt P53853 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3C9D 2.0 Å, Crystal structure of Vps75
3DM7 2.0 Å, Crystal Structure of the Vps75 Histone Chaperone
3C9B 2.42 Å, Crystal structure of SeMet Vps75
3Q66 2.71 Å, Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex…
3Q68 2.71 Å, Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex…
3Q33 2.8 Å, Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated…
3Q35 3.3 Å, Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated…
5AGC 4.0 Å, Crystallographic forms of the Vps75 tetramer
6O22 Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex…

Browse structure collections

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