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Open-gate mycobacterium 20S cp proteasome in complex mpa - global 3D refinement

Analyse Open-gate mycobacterium 20S cp proteasome in complex mpa - global 3D refinement in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PXA
Type: protein
Length: 6,187 residues
Chains: 35
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proteasome subunit alpha; Aaa ATPase forming ring-shaped complexes; Proteasome subunit…
EC: 3.4.25.1
UniProt: A0A655IUE1, A0A045JPX7, A0A045HFG5
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 9 distinct chains · 41% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
0, 2, 4, 6, 8, O, Q, Z, d, f	Proteasome subunit alpha	protein	215	40% helix, 25% strand	A0A655IUE1
1, A, B, D	Aaa ATPase forming ring-shaped complexes	protein	5	0% helix, 20% strand	A0A045JPX7
C, E	Aaa ATPase forming ring-shaped complexes	protein	7	0% helix, 14% strand	A0A045JPX7
F	Aaa ATPase forming ring-shaped complexes	protein	6	0% helix, 17% strand	A0A045JPX7
H, L, M, N, R, S	Proteasome subunit beta (EC 3.4.25.1)	protein	222	41% helix, 30% strand	A0A045HFG5
I, T, X	Proteasome subunit alpha	protein	214	43% helix, 24% strand	A0A655IUE1
J, P, V, Y, a, b	Proteasome subunit beta (EC 3.4.25.1)	protein	223	40% helix, 30% strand	A0A045HFG5
K	Proteasome subunit alpha	protein	217	43% helix, 24% strand	A0A655IUE1
U, W	Proteasome subunit beta (EC 3.4.25.1)	protein	234	41% helix, 29% strand	A0A045HFG5

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	989	0.87	0.89	109	empty
2	1164	0.85	0.86	111	empty
3	1164	0.84	0.85	103	empty
4	563	0.83	0.89	46	empty
5	591	0.83	0.88	46	empty

Interfaces

84 interfaces between chains.

N–U · 812 Å² buried · 17 hydrogen bonds · protein-protein
L–W · 811 Å² buried · 15 hydrogen bonds · protein-protein
Y–b · 758 Å² buried · 15 hydrogen bonds · protein-protein
H–J · 755 Å² buried · 16 hydrogen bonds · protein-protein
R–S · 751 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

7PXA · Open-gate mycobacterium 20S CP proteasome in complex MPA - global 3D refinement · the same entry in another collection · chain 1 against 1, 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 A0A655IUE1
Every structure of UniProt A0A045JPX7
Every structure of UniProt A0A045HFG5
Elsewhere: RCSB PDB 7PXA · PDBe 7PXA · UniProt A0A655IUE1 · UniProt A0A045JPX7 · UniProt A0A045HFG5

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