MolNFT v1 · #68318 · protein

Crystal structure of archaeal 20S proteasome in complex with mutated P26 activator

3JSE · Proteasome subunit alpha: “Crystal structure of archaeal 20S proteasome in complex with mutated P26 activator”. X-ray diffraction, 20 pockets (best druggability 0.83). MolNFT v1 #68318 on GenesisL1: 3D structure, binding sites and…

PDB: 3JSE
Type: protein
Length: 4,536 residues
Chains: 21
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proteasome subunit alpha; Proteasome subunit beta; Proteasome activator protein PA26
EC: 3.4.25.1
UniProt: P25156, P28061, Q9U8G2
Pockets: 20 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 48% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	Proteasome subunit alpha (EC 3.4.25.1)	protein	227	33% helix, 26% strand	P25156
H, I, J, K, L, M, N	Proteasome subunit beta (EC 3.4.25.1)	protein	203	37% helix, 31% strand	P28061
O, P, Q, R, S, T, U	Proteasome activator protein PA26	protein	218	73% helix, 2% strand	Q9U8G2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1050	0.83	0.84	116	empty
2	1134	0.82	0.84	127	empty
3	1190	0.82	0.83	124	empty
4	1117	0.81	0.83	115	empty
5	1154	0.81	0.82	125	empty

Interfaces

56 interfaces between chains.

S–T · 2182 Å² buried · 43 hydrogen bonds · protein-protein
T–U · 2161 Å² buried · 42 hydrogen bonds · protein-protein
P–Q · 2160 Å² buried · 37 hydrogen bonds · protein-protein
O–P · 2153 Å² buried · 37 hydrogen bonds · protein-protein
Q–R · 2151 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

3JSE · Crystal structure of archaeal 20S proteasome in complex with mutated P26 activator · the same entry in another collection · chain U against U, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P25156
Every structure of UniProt P28061
Every structure of UniProt Q9U8G2
Elsewhere: RCSB PDB 3JSE · PDBe 3JSE · UniProt P25156 · UniProt P28061 · UniProt Q9U8G2

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