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Structure of recombinant human gamma-tubulin ring complex 10-spoked assembly intermediate (spokes 3-12, substoichiometric spokes 13-14)

Analyse Structure of recombinant human gamma-tubulin ring complex 10-spoked assembly… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QJ6
Type: protein
Length: 11,334 residues
Chains: 31
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Actin, cytoplasmic 1; Mitotic-spindle organizing protein 1; Gamma-tubulin complex…
UniProt: A0A6I9HGD1, Q08AG7, Q96CW5, Q9BSJ2, Q9UGJ1, Q96RT8, Q96RT7, P23258
Pockets: 20 · best druggability 0.90

Structure

electron microscopy · 18 distinct chains · 60% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
e	Actin, cytoplasmic 1	protein	364	43% helix, 15% strand	A0A6I9HGD1
b, k, m, i	Mitotic-spindle organizing protein 1	protein	65	71% helix, 0% strand	Q08AG7
a	Gamma-tubulin complex component 3	protein	116	53% helix, 0% strand	Q96CW5
C	Gamma-tubulin complex component 2	protein	620	56% helix, 3% strand	Q9BSJ2
D	Gamma-tubulin complex component 3	protein	581	64% helix, 4% strand	Q96CW5
E	Gamma-tubulin complex component 2	protein	638	58% helix, 2% strand	Q9BSJ2
F	Gamma-tubulin complex component 3	protein	599	59% helix, 3% strand	Q96CW5
G	Gamma-tubulin complex component 2	protein	640	59% helix, 3% strand	Q9BSJ2
H	Gamma-tubulin complex component 3	protein	594	69% helix, 3% strand	Q96CW5
I	Gamma-tubulin complex component 4	protein	521	62% helix, 2% strand	Q9UGJ1
J	Gamma-tubulin complex component 5	protein	534	65% helix, 0% strand	Q96RT8
K	Gamma-tubulin complex component 4	protein	562	68% helix, 1% strand	Q9UGJ1
L	Gamma-tubulin complex component 6	protein	566	59% helix, 1% strand	Q96RT7
Q, R, S, T, U, V, W, X, Y, Z	Tubulin gamma-1 chain	protein	420	43% helix, 16% strand	P23258
d	Mitotic-spindle organizing protein 1	protein	59	73% helix, 0% strand	Q08AG7
c	Gamma-tubulin complex component 6	protein	158	54% helix, 0% strand	Q96RT7
h, j	Gamma-tubulin complex component 3	protein	107	58% helix, 0% strand	Q96CW5
l	Gamma-tubulin complex component 5	protein	108	67% helix, 0% strand	Q96RT8

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	1171	0.90	0.91	158	empty
2	798	0.88	0.91	136	empty
3	1166	0.86	0.87	159	empty
4	880	0.86	0.88	97	empty
5	1067	0.85	0.86	158	empty

Interfaces

63 interfaces between chains.

i–h · 2884 Å² buried · 35 hydrogen bonds · protein-protein
F–T · 2277 Å² buried · 15 hydrogen bonds · protein-protein
K–L · 2274 Å² buried · 18 hydrogen bonds · protein-protein
k–j · 2256 Å² buried · 8 hydrogen bonds · protein-protein
H–V · 2240 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

7QJ6 · Structure of recombinant human gamma-Tubulin Ring Complex 10-spoked assembly intermediate… · 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 A0A6I9HGD1
Every structure of UniProt Q08AG7
Every structure of UniProt Q96CW5
Every structure of UniProt Q9BSJ2
Every structure of UniProt Q9UGJ1
Every structure of UniProt Q96RT8
Every structure of UniProt Q96RT7
Every structure of UniProt P23258
Elsewhere: RCSB PDB 7QJ6 · PDBe 7QJ6 · UniProt A0A6I9HGD1 · UniProt Q08AG7 · UniProt Q96CW5 · UniProt Q9BSJ2 · UniProt Q9UGJ1 · UniProt Q96RT8 · UniProt Q96RT7 · UniProt P23258

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