MolNFT v1 · #85070 · protein

Model built against symmetry-free cryo-EM MAP of tric-ADP-alfx

4A0W · T-complex protein 1 subunit beta: “Model built against symmetry-free cryo-EM MAP of tric-ADP-alfx”. Electron microscopy, 20 pockets (best druggability 0.89). MolNFT v1 #85070 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4A0W
Type: protein
Length: 8,076 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T-complex protein 1 subunit beta
UniProt: Q3ZBH0
Pockets: 20 · best druggability 0.89

Structure

electron microscopy · 6 distinct chains · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E, F, G, I, J, M, P	T-complex protein 1 subunit beta	protein	513	48% helix, 13% strand	Q3ZBH0
C	T-complex protein 1 subunit beta	protein	490	48% helix, 13% strand	Q3ZBH0
H	T-complex protein 1 subunit beta	protein	492	48% helix, 12% strand	Q3ZBH0
K	T-complex protein 1 subunit beta	protein	491	48% helix, 11% strand	Q3ZBH0
L, O	T-complex protein 1 subunit beta	protein	490	48% helix, 11% strand	Q3ZBH0
N	T-complex protein 1 subunit beta	protein	493	48% helix, 10% strand	Q3ZBH0

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	905	0.89	0.92	147	empty
2	1147	0.87	0.88	144	empty
3	783	0.87	0.90	134	empty
4	1133	0.87	0.88	136	empty
5	1059	0.87	0.88	155	empty

Interfaces

32 interfaces between chains.

B–F · 1355 Å² buried · 0 hydrogen bonds · protein-protein
D–H · 1320 Å² buried · 4 hydrogen bonds · protein-protein
B–G · 1233 Å² buried · 4 hydrogen bonds · protein-protein
E–G · 1227 Å² buried · 3 hydrogen bonds · protein-protein
D–E · 1147 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

Q3ZBH0 · AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit beta (Q3ZBH0) · a predicted model of the same protein · chain H against A, TM-score 0.85

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 Q3ZBH0
Elsewhere: RCSB PDB 4A0W · PDBe 4A0W · UniProt Q3ZBH0

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