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The crystal structures of the eukaryotic chaperonin cct reveal its functional partitioning

Analyse The crystal structures of the eukaryotic chaperonin cct reveal its functional… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4B2T
Type: protein
Length: 6,842 residues
Chains: 16
Method: x-ray diffraction
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: Q32L40, Q3ZBH0, Q2T9X2, Q3T0K2, Q2NKZ1, Q3ZCI9, Q3MHL7
Pockets: 20 · best druggability 0.83

Structure

x-ray diffraction · 15 distinct chains · 51% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T-complex protein 1 subunit alpha	protein	481	48% helix, 15% strand	Q32L40
B	T-complex protein 1 subunit beta	protein	481	50% helix, 15% strand	Q3ZBH0
D	T-complex protein 1 subunit delta	protein	481	48% helix, 14% strand	Q2T9X2
E	T-complex protein 1 subunit epsilon	protein	481	47% helix, 14% strand	—
G	T-complex protein 1 subunit gamma	protein	481	47% helix, 14% strand	Q3T0K2
H	T-complex protein 1 subunit eta	protein	481	46% helix, 15% strand	Q2NKZ1
Q	T-complex protein 1 subunit theta	protein	481	50% helix, 15% strand	Q3ZCI9
Z, z	T-complex protein 1 subunit zeta	protein	481	48% helix, 14% strand	Q3MHL7
a	T-complex protein 1 subunit alpha	protein	359	52% helix, 8% strand	Q32L40
b	T-complex protein 1 subunit beta	protein	359	60% helix, 11% strand	Q3ZBH0
d	T-complex protein 1 subunit delta	protein	359	57% helix, 10% strand	Q2T9X2
e	T-complex protein 1 subunit epsilon	protein	359	56% helix, 11% strand	—
g	T-complex protein 1 subunit gamma	protein	359	57% helix, 9% strand	Q3T0K2
h	T-complex protein 1 subunit eta	protein	359	55% helix, 9% strand	Q2NKZ1
q	T-complex protein 1 subunit theta	protein	359	57% helix, 9% strand	Q3ZCI9

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	980	0.83	0.84	88	empty
2	382	0.83	0.92	58	empty
3	949	0.83	0.84	77	empty
4	465	0.82	0.90	49	empty
5	708	0.82	0.86	59	empty

Interfaces

32 interfaces between chains.

E–H · 1608 Å² buried · 12 hydrogen bonds · protein-protein
a–g · 1381 Å² buried · 18 hydrogen bonds · protein-protein
e–h · 1334 Å² buried · 16 hydrogen bonds · protein-protein
G–Z · 1301 Å² buried · 15 hydrogen bonds · protein-protein
b–e · 1256 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4B2T · The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning · the same entry in another collection · chain H against H, 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 Q32L40
Every structure of UniProt Q3ZBH0
Every structure of UniProt Q2T9X2
Every structure of UniProt Q3T0K2
Every structure of UniProt Q2NKZ1
Every structure of UniProt Q3ZCI9
Every structure of UniProt Q3MHL7
Elsewhere: RCSB PDB 4B2T · PDBe 4B2T · UniProt Q32L40 · UniProt Q3ZBH0 · UniProt Q2T9X2 · UniProt Q3T0K2 · UniProt Q2NKZ1 · UniProt Q3ZCI9 · UniProt Q3MHL7

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