5AGC: Crystallographic forms of the Vps75 tetramer

Crystallographic forms of the Vps75 tetramer. Determined by X-ray diffraction at 4.0 Å resolution. Released 2 Mar 2016.

Method: X-ray diffraction
Resolution: 4.0 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 4
Atoms: 7,250
Mol. weight: 122.62 kDa
Released: 2 Mar 2016

Explore 5AGC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5AGC contains 48 α-helices and 24 β-strands across 4 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	10-51	42
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	209-222	14

Chain B: 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	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	150-155	6
α-helix	166-176	11
α-helix	179-182	4
α-helix	197-202	6
α-helix	203-208	6
α-helix	209-220	12

Chains C and D: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	11-51	41
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	5
α-helix	91-93	3
β-strand	103-109	7	5
β-strand	112	1	6
β-strand	116	1	6
β-strand	119-128	10	5
β-strand	138-141	4	5
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	209-222	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vacuolar protein sorting-associated protein 75	A, B, C, D	protein	264	SACCHAROMYCES CEREVISIAE	P53853 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5AGC_1 VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 75 (chains A, B, C, D)
MMSDQENENEHAKAFLGLAKCEEEVDAIEREVELYRLNKMKPVYEKRDAYIDEIAEFWKI
VLSQHVSFANYIRASDFKYIDTIDKIKVEWLALESEMYDTRDFSITFHFHGIEGDFKEQQ
VTKVFQIKKGKDDQEDGILTSEPVPIEWPQSYDSINPDLIKDKRSPEGKKKYRQGMKTIF
GWFRWTGLKPGKEFPHGDSLASLFSEEIYPFCVKYYAEAQRDLEDEEGESGLSADGDSED
DDGSLGEVDLPLSDEEPSSKKRKV

Primary citation

The Histone Chaperone Vps75 Forms Multiple Oligomeric Assemblies Capable of Mediating Exchange between Histone H3-H4 Tetramers and Asf1-H3-H4 Complexes. Hammond, C.M., Sundaramoorthy, R., Larance, M. et al. Nucleic Acids Res (2016) 44:6157. DOI 10.1093/NAR/GKW209 · PubMed

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

2ZD7 1.85 Å, The structure of VPS75 (Vacuolar protein sorting-associated protein 75)
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…
6O22 Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex…

Browse structure collections

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