MolNFT v1 · #67617 · protein

Crystal structure of archaeal 20S proteasome in complex with the C- terminus of pan

3IPM · Proteasome subunit alpha: “Crystal structure of archaeal 20S proteasome in complex with the C- terminus of pan”. X-ray diffraction, 20 pockets (best druggability 0.81). MolNFT v1 #67617 on GenesisL1: 3D structure, binding sites and…

PDB: 3IPM
Type: protein
Length: 4,543 residues
Chains: 21
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proteasome subunit alpha; Proteasome subunit beta; Proteasome activator PA26…
EC: 3.4.25.1
UniProt: P25156, P28061, Q38BM8, Q58576
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 3 distinct chains · 46% helix, 15% 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	31% helix, 22% strand	P25156
H, I, J, K, L, M, N	Proteasome subunit beta (EC 3.4.25.1)	protein	203	34% helix, 24% strand	P28061
O, P, Q, R, S, T, U	Proteasome activator PA26, proteasome-activating nucleotidase fusion protein	protein	219	73% helix, 0% strand	Q38BM8, Q58576

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	566	0.81	0.87	74	empty
2	571	0.81	0.87	63	empty
3	549	0.81	0.87	61	empty
4	639	0.80	0.85	80	empty
5	627	0.80	0.85	77	empty

Interfaces

56 interfaces between chains.

P–Q · 2091 Å² buried · 22 hydrogen bonds · protein-protein
O–P · 2079 Å² buried · 23 hydrogen bonds · protein-protein
R–S · 2076 Å² buried · 20 hydrogen bonds · protein-protein
T–U · 2069 Å² buried · 21 hydrogen bonds · protein-protein
S–T · 2069 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

3IPM · Crystal Structure of Archaeal 20S Proteasome in Complex with the C-terminus of PAN · the same entry in another collection · chain S against S, 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 Q38BM8
Every structure of UniProt Q58576
Elsewhere: RCSB PDB 3IPM · PDBe 3IPM · UniProt P25156 · UniProt P28061 · UniProt Q38BM8 · UniProt Q58576

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