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Crystal structure of the 20S proteasome from yeast at 2.4 ångströms resolution

Analyse Crystal structure of the 20S proteasome from yeast at 2.4 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1RYP
Type
protein
Length
6,386 residues
Chains
28
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
20S proteasome
EC
3.4.99.46
UniProt
P21243, P23639, P23638, P40303, P32379, P40302, P21242, P38624, P25043, P25451, P22141, P30656, P23724, P30657
Ligands
MG
Pockets
20 · best druggability 0.84

Structure

x-ray diffraction · 14 distinct chains · 35% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, O20S proteasome (EC 3.4.99.46)protein24340% helix, 23% strandP21243
B, P20S proteasome (EC 3.4.99.46)protein25035% helix, 26% strandP23639
C, Q20S proteasome (EC 3.4.99.46)protein24438% helix, 25% strandP23638
D, R20S proteasome (EC 3.4.99.46)protein24136% helix, 24% strandP40303
E, S20S proteasome (EC 3.4.99.46)protein24235% helix, 26% strandP32379
F, T20S proteasome (EC 3.4.99.46)protein23338% helix, 27% strandP40302
G, U20S proteasome (EC 3.4.99.46)protein24438% helix, 26% strandP21242
H, V20S proteasome (EC 3.4.99.46)protein20535% helix, 35% strandP38624
I, W20S proteasome (EC 3.4.99.46)protein22229% helix, 34% strandP25043
J, X20S proteasome (EC 3.4.99.46)protein20432% helix, 32% strandP25451
K, Y20S proteasome (EC 3.4.99.46)protein19834% helix, 33% strandP22141
L, Z20S proteasome (EC 3.4.99.46)protein21236% helix, 33% strandP30656
M, 120S proteasome (EC 3.4.99.46)protein22228% helix, 32% strandP23724
N, 220S proteasome (EC 3.4.99.46)protein23332% helix, 31% strandP30657

Ligands and binding sites

  • MG · Magnesium ion · metal · 20 copies · chains A, B, G, E, M, H, 2, I, 1, J, L, X, O, P, U, S, N, V, W, Z

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110830.840.85131MG
210710.800.81111empty
39510.800.82103empty
410480.800.81116MG
57080.800.8493empty

Interfaces

92 interfaces between chains.

  • W–X · 1700 Ų buried · 28 hydrogen bonds · protein-protein
  • I–J · 1681 Ų buried · 28 hydrogen bonds · protein-protein
  • C–D · 1671 Ų buried · 25 hydrogen bonds · protein-protein
  • Q–R · 1631 Ų buried · 22 hydrogen bonds · protein-protein
  • I–1 · 1495 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 1RYP · Crystal structure of the 20S proteasome from yeast at 2.4 ångströms resolution · the same entry in another collection · chain B against B, TM-score 1.00

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