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Mouse PA28ALPHA-beta

Analyse Mouse PA28ALPHA-beta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MX5
Type: protein
Length: 2,929 residues
Chains: 14
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proteasome activator complex subunit 1; Proteasome activator complex subunit 2
UniProt: P97371, P97372
Ligands: PO4
Pockets: 20 · best druggability 0.77

Structure

x-ray diffraction · 14 distinct chains · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proteasome activator complex subunit 1	protein	208	77% helix, 1% strand	P97371
B	Proteasome activator complex subunit 2	protein	209	75% helix, 1% strand	P97372
C	Proteasome activator complex subunit 1	protein	213	76% helix, 1% strand	P97371
D	Proteasome activator complex subunit 2	protein	212	74% helix, 1% strand	P97372
E	Proteasome activator complex subunit 1	protein	211	74% helix, 1% strand	P97371
F	Proteasome activator complex subunit 2	protein	216	73% helix, 1% strand	P97372
G	Proteasome activator complex subunit 1	protein	208	76% helix, 1% strand	P97371
H	Proteasome activator complex subunit 1	protein	206	76% helix, 1% strand	P97371
I	Proteasome activator complex subunit 2	protein	204	76% helix, 1% strand	P97372
J	Proteasome activator complex subunit 1	protein	202	77% helix, 1% strand	P97371
K	Proteasome activator complex subunit 2	protein	210	75% helix, 1% strand	P97372
L	Proteasome activator complex subunit 1	protein	214	75% helix, 1% strand	P97371
M	Proteasome activator complex subunit 2	protein	211	74% helix, 1% strand	P97372
N	Proteasome activator complex subunit 1	protein	205	77% helix, 1% strand	P97371

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains E, G, N

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	691	0.77	0.82	80	empty
2	640	0.76	0.82	70	empty
3	1023	0.76	0.78	135	empty
4	517	0.75	0.83	59	empty
5	560	0.75	0.82	56	empty

Interfaces

23 interfaces between chains.

E–F · 2250 Å² buried · 24 hydrogen bonds · protein-protein
D–E · 2138 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 2118 Å² buried · 21 hydrogen bonds · protein-protein
A–G · 2116 Å² buried · 21 hydrogen bonds · protein-protein
F–G · 2110 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5MX5 · Mouse PA28alpha-beta · the same entry in another collection · chain K against K, 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 P97371
Every structure of UniProt P97372
Elsewhere: RCSB PDB 5MX5 · PDBe 5MX5 · UniProt P97371 · UniProt P97372

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