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Yeast 20S PROTEASOME:SYRINGOLIN a-complex

Analyse Yeast 20S PROTEASOME:SYRINGOLIN a-complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZCY
Type
protein
Length
6,368 residues
Chains
28
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Proteasome component Y7; Proteasome component Y13; Proteasome component PRE6; Proteasome…
EC
3.4.25.1
UniProt
P23639, P23638, P40303, P32379, P40302, P21242, P21243, P25043, P25451, P22141, P30656, P23724, P30657, P38624
Ligands
SRG
Pockets
20 · best druggability 0.82

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, OProteasome component Y7 (EC 3.4.25.1)protein25036% helix, 26% strandP23639
B, PProteasome component Y13 (EC 3.4.25.1)protein24438% helix, 25% strandP23638
C, QProteasome component PRE6 (EC 3.4.25.1)protein24137% helix, 24% strandP40303
D, RProteasome component PUP2 (EC 3.4.25.1)protein24237% helix, 26% strandP32379
E, SProteasome component PRE5 (EC 3.4.25.1)protein23337% helix, 28% strandP40302
F, TProteasome component C1 (EC 3.4.25.1)protein24438% helix, 27% strandP21242
G, UProteasome component C7-alpha (EC 3.4.25.1)protein24339% helix, 23% strandP21243
H, VProteasome component PUP1 (EC 3.4.25.1)protein22229% helix, 35% strandP25043
I, WProteasome component PUP3 (EC 3.4.25.1)protein20432% helix, 33% strandP25451
J, XProteasome component C11 (EC 3.4.25.1)protein19832% helix, 33% strandP22141
K, YProteasome component PRE2 (EC 3.4.25.1)protein21235% helix, 33% strandP30656
L, ZProteasome component C5 (EC 3.4.25.1)protein22228% helix, 32% strandP23724
M, 0Proteasome component PRE4 (EC 3.4.25.1)protein23332% helix, 30% strandP30657
N, 1Proteasome component PRE3 (EC 3.4.25.1)protein19637% helix, 35% strandP38624

Ligands and binding sites

  • SRG · (2S)-2-[[(2S)-1-[[(5S,8S,9E)-2,7-dioxo-5-propan-2-yl-1,6-diazacyclododeca-3,9-dien-8-yl]amino]-3-methyl-1-oxo-butan-2-yl]carbamoylamino]-3-methyl-butanoic acid · ligand · 6 copies · chains H, I, K, L, N, V, W, Y, Z, 1

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
19130.820.84124SRG
28270.810.8487empty
39450.810.8392empty
411530.810.82108empty
511330.810.8296empty

Interfaces

92 interfaces between chains.

  • V–W · 1687 Ų buried · 26 hydrogen bonds · protein-protein
  • H–I · 1686 Ų buried · 26 hydrogen bonds · protein-protein
  • B–C · 1623 Ų buried · 26 hydrogen bonds · protein-protein
  • P–Q · 1587 Ų buried · 25 hydrogen bonds · protein-protein
  • O–U · 1465 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 covalent (covalent ligand).

Compared structures

  • 2ZCY · yeast 20S proteasome:syringolin A-complex · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

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