Research workbench

Human CCT:MLST8 complex

Analyse Human CCT:MLST8 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6QB8
Type: protein
Length: 7,870 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: P17987, P78371, P50991, P48643, P49368, Q99832, P50990, P40227
Ligands: ADP
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 15 distinct chains · 46% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
a	T-complex protein 1 subunit alpha	protein	490	41% helix, 13% strand	P17987
b	T-complex protein 1 subunit beta	protein	478	48% helix, 9% strand	P78371
d	T-complex protein 1 subunit delta	protein	489	49% helix, 11% strand	P50991
e	T-complex protein 1 subunit epsilon	protein	505	45% helix, 7% strand	P48643
g	T-complex protein 1 subunit gamma	protein	477	47% helix, 12% strand	P49368
h	T-complex protein 1 subunit eta	protein	500	45% helix, 13% strand	Q99832
q, Q	T-complex protein 1 subunit theta	protein	483	50% helix, 9% strand	P50990
z	T-complex protein 1 subunit zeta	protein	508	49% helix, 13% strand	P40227
A	T-complex protein 1 subunit alpha	protein	494	44% helix, 12% strand	P17987
B	T-complex protein 1 subunit beta	protein	492	48% helix, 9% strand	P78371
D	T-complex protein 1 subunit delta	protein	487	49% helix, 10% strand	P50991
E	T-complex protein 1 subunit epsilon	protein	503	46% helix, 5% strand	P48643
G	T-complex protein 1 subunit gamma	protein	485	44% helix, 12% strand	P49368
H	T-complex protein 1 subunit eta	protein	499	44% helix, 11% strand	Q99832
Z	T-complex protein 1 subunit zeta	protein	497	46% helix, 13% strand	P40227

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains q, Q

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	1010	0.84	0.85	92	empty
2	1127	0.84	0.85	109	empty
3	1187	0.84	0.85	108	empty
4	1147	0.83	0.84	107	empty
5	958	0.83	0.84	99	ADP

Interfaces

30 interfaces between chains.

e–h · 1606 Å² buried · 23 hydrogen bonds · protein-protein
E–H · 1494 Å² buried · 11 hydrogen bonds · protein-protein
h–q · 1343 Å² buried · 24 hydrogen bonds · protein-protein
H–Q · 1306 Å² buried · 24 hydrogen bonds · protein-protein
q–z · 1253 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6QB8 · Human CCT:mLST8 complex · the same entry in another collection · chain D against D, 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 P17987
Every structure of UniProt P78371
Every structure of UniProt P50991
Every structure of UniProt P48643
Every structure of UniProt P49368
Every structure of UniProt Q99832
Every structure of UniProt P50990
Every structure of UniProt P40227
Elsewhere: RCSB PDB 6QB8 · PDBe 6QB8 · UniProt P17987 · UniProt P78371 · UniProt P50991 · UniProt P48643 · UniProt P49368 · UniProt Q99832 · UniProt P50990 · UniProt P40227

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.