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Structure of recombinant human gamma-tubulin ring complex 10-spoked assembly intermediate (spokes 5-14)

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: 7QJ4
Type: protein
Length: 10,766 residues
Chains: 28
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin gamma-1 chain; Gamma-tubulin complex component 5; Gamma-tubulin complex component…
UniProt: P23258, Q96RT8, Q96CW5, Q08AG7, Q9BSJ2, Q9UGJ1, Q96RT7
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 14 distinct chains · 60% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1, 2, S, T, U, V, W, X, Y, Z	Tubulin gamma-1 chain	protein	420	42% helix, 16% strand	P23258
l	Gamma-tubulin complex component 5	protein	108	67% helix, 0% strand	Q96RT8
n, j	Gamma-tubulin complex component 3	protein	99	62% helix, 0% strand	Q96CW5
o, m, k, b	Mitotic-spindle organizing protein 1	protein	65	71% helix, 0% strand	Q08AG7
E	Gamma-tubulin complex component 2	protein	638	56% helix, 2% strand	Q9BSJ2
F	Gamma-tubulin complex component 3	protein	599	59% helix, 1% strand	Q96CW5
G	Gamma-tubulin complex component 2	protein	640	58% helix, 3% strand	Q9BSJ2
H, N	Gamma-tubulin complex component 3	protein	594	67% helix, 3% strand	Q96CW5
I	Gamma-tubulin complex component 4	protein	521	61% helix, 2% strand	Q9UGJ1
J	Gamma-tubulin complex component 5	protein	534	65% helix, 1% strand	Q96RT8
K	Gamma-tubulin complex component 4	protein	562	66% helix, 3% strand	Q9UGJ1
L	Gamma-tubulin complex component 6	protein	566	59% helix, 0% strand	Q96RT7
M	Gamma-tubulin complex component 2	protein	636	58% helix, 4% strand	Q9BSJ2
a	Gamma-tubulin complex component 3	protein	116	53% helix, 0% strand	Q96CW5

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	788	0.87	0.89	87	empty
2	931	0.86	0.88	117	empty
3	1146	0.85	0.86	127	empty
4	784	0.85	0.88	77	empty
5	653	0.85	0.89	93	empty

Interfaces

54 interfaces between chains.

2–N · 2660 Å² buried · 33 hydrogen bonds · protein-protein
1–M · 2612 Å² buried · 37 hydrogen bonds · protein-protein
E–S · 2336 Å² buried · 25 hydrogen bonds · protein-protein
n–o · 2272 Å² buried · 16 hydrogen bonds · protein-protein
K–L · 2270 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

7QJ4 · Structure of recombinant human gamma-Tubulin Ring Complex 10-spoked assembly intermediate… · 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 P23258
Every structure of UniProt Q96RT8
Every structure of UniProt Q96CW5
Every structure of UniProt Q08AG7
Every structure of UniProt Q9BSJ2
Every structure of UniProt Q9UGJ1
Every structure of UniProt Q96RT7
Elsewhere: RCSB PDB 7QJ4 · PDBe 7QJ4 · UniProt P23258 · UniProt Q96RT8 · UniProt Q96CW5 · UniProt Q08AG7 · UniProt Q9BSJ2 · UniProt Q9UGJ1 · UniProt Q96RT7

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