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Symmetry-free cryo-EM MAP of tric in the nucleotide-free (apo) state

Analyse Symmetry-free cryo-EM MAP of tric in the nucleotide-free (apo) state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4A0O
Type: protein
Length: 7,587 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 0.88

Structure

electron microscopy · 15 distinct chains · 48% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T-complex protein 1 subunit beta	protein	339	58% helix, 6% strand	Q3ZBH0
B	T-complex protein 1 subunit beta	protein	490	47% helix, 12% strand	Q3ZBH0
C	T-complex protein 1 subunit beta	protein	482	47% helix, 11% strand	Q3ZBH0
D	T-complex protein 1 subunit beta	protein	489	48% helix, 11% strand	Q3ZBH0
E	T-complex protein 1 subunit beta	protein	492	49% helix, 12% strand	Q3ZBH0
F	T-complex protein 1 subunit beta	protein	488	49% helix, 13% strand	Q3ZBH0
G	T-complex protein 1 subunit beta	protein	513	47% helix, 12% strand	Q3ZBH0
H	T-complex protein 1 subunit beta	protein	493	47% helix, 10% strand	Q3ZBH0
I	T-complex protein 1 subunit beta	protein	473	45% helix, 10% strand	Q3ZBH0
J	T-complex protein 1 subunit beta	protein	490	49% helix, 13% strand	Q3ZBH0
K, P	T-complex protein 1 subunit beta	protein	496	49% helix, 10% strand	Q3ZBH0
L	T-complex protein 1 subunit beta	protein	491	47% helix, 11% strand	Q3ZBH0
M	T-complex protein 1 subunit beta	protein	388	51% helix, 12% strand	Q3ZBH0
N	T-complex protein 1 subunit beta	protein	486	46% helix, 13% strand	Q3ZBH0
O	T-complex protein 1 subunit beta	protein	481	47% helix, 12% 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	946	0.88	0.89	129	empty
2	549	0.88	0.93	96	empty
3	893	0.87	0.89	114	empty
4	635	0.87	0.91	100	empty
5	999	0.86	0.87	104	empty

Interfaces

39 interfaces between chains.

L–P · 2003 Å² buried · 13 hydrogen bonds · protein-protein
B–F · 1990 Å² buried · 17 hydrogen bonds · protein-protein
D–H · 1359 Å² buried · 3 hydrogen bonds · protein-protein
I–N · 1354 Å² buried · 9 hydrogen bonds · protein-protein
J–K · 1347 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

4A0O · Symmetry-free cryo-EM map of TRiC in the nucleotide-free (apo) state · 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 Q3ZBH0
Elsewhere: RCSB PDB 4A0O · PDBe 4A0O · UniProt Q3ZBH0

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