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Tric at 0.05 mm ADP-alfx, conformation 4, 0.05-C4

Analyse Tric at 0.05 mm ADP-alfx, conformation 4, 0.05-C4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KRD
Type: protein
Length: 8,006 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T-complex protein 1 subunit alpha; T-complex protein 1 subunit beta; T-complex protein 1…
UniProt: P12612, P39076, P39078, P40413, P39077, P47079, P39079, P42943
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 15 distinct chains · 47% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
a	T-complex protein 1 subunit alpha	protein	511	47% helix, 13% strand	P12612
A	T-complex protein 1 subunit alpha	protein	513	45% helix, 12% strand	P12612
b	T-complex protein 1 subunit beta	protein	502	48% helix, 14% strand	P39076
B	T-complex protein 1 subunit beta	protein	504	48% helix, 16% strand	P39076
d	T-complex protein 1 subunit delta	protein	480	49% helix, 12% strand	P39078
D	T-complex protein 1 subunit delta	protein	429	51% helix, 12% strand	P39078
e	T-complex protein 1 subunit epsilon	protein	501	47% helix, 10% strand	P40413
E	T-complex protein 1 subunit epsilon	protein	495	44% helix, 10% strand	P40413
g	T-complex protein 1 subunit gamma	protein	493	47% helix, 8% strand	P39077
G	T-complex protein 1 subunit gamma	protein	462	47% helix, 8% strand	P39077
q	T-complex protein 1 subunit theta	protein	524	43% helix, 13% strand	P47079
Q	T-complex protein 1 subunit theta	protein	523	44% helix, 12% strand	P47079
z	T-complex protein 1 subunit zeta	protein	524	48% helix, 9% strand	P39079
Z	T-complex protein 1 subunit zeta	protein	531	49% helix, 10% strand	P39079
h, H	T-complex protein 1 subunit eta	protein	507	46% helix, 12% strand	P42943

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	712	0.87	0.91	101	empty
2	764	0.87	0.90	103	empty
3	1125	0.87	0.88	118	empty
4	708	0.86	0.90	95	empty
5	915	0.86	0.88	109	empty

Interfaces

34 interfaces between chains.

e–h · 3371 Å² buried · 43 hydrogen bonds · protein-protein
E–H · 3130 Å² buried · 37 hydrogen bonds · protein-protein
b–e · 2203 Å² buried · 19 hydrogen bonds · protein-protein
B–E · 2031 Å² buried · 26 hydrogen bonds · protein-protein
Q–Z · 1616 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

6KRD · TRiC at 0.05 mM ADP-AlFx, Conformation 4, 0.05-C4 · the same entry in another collection · chain G against G, 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 P12612
Every structure of UniProt P39076
Every structure of UniProt P39078
Every structure of UniProt P40413
Every structure of UniProt P39077
Every structure of UniProt P47079
Every structure of UniProt P39079
Every structure of UniProt P42943
Elsewhere: RCSB PDB 6KRD · PDBe 6KRD · UniProt P12612 · UniProt P39076 · UniProt P39078 · UniProt P40413 · UniProt P39077 · UniProt P47079 · UniProt P39079 · UniProt P42943

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