Research workbench

Tubulin-7-aminonoscapine complex

Analyse Tubulin-7-aminonoscapine complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Y6D
Type: protein
Length: 2,177 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin alpha-1B chain; Tubulin beta-2B chain; Stathmin-4; Tubulin-tyrosine ligase
UniProt: P81947, Q6B856, P63043, E1BQ43
Ligands: GTP, GDP, OBQ, ACP, MG, CA
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 6 distinct chains · 47% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tubulin alpha-1B chain	protein	439	45% helix, 18% strand	P81947
B	Tubulin beta-2B chain	protein	422	49% helix, 20% strand	Q6B856
C	Tubulin alpha-1B chain	protein	440	46% helix, 17% strand	P81947
D	Tubulin beta-2B chain	protein	421	49% helix, 19% strand	Q6B856
E	Stathmin-4	protein	122	78% helix, 14% strand	P63043
F	Tubulin-tyrosine ligase	protein	333	33% helix, 23% strand	E1BQ43

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B, C, D
GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains B, D
OBQ · (3~{S})-7-azanyl-6-methoxy-3-[(5~{R})-4-methoxy-6-methyl-7,8-dihydro-5~{H}-[1,3]dioxolo[4,5-g]isoquinolin-5-yl]-3~{H}-2-benzofuran-1-one · ligand · 2 copies · chains A, B, C, D
ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains F
MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, F
CA · Calcium ion · metal · 2 copies · chains A, C
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A, B
GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	953	0.86	0.87	115	GTP, MG, OBQ
2	887	0.83	0.85	125	GDP, MG, GOL
3	633	0.79	0.84	70	OBQ
4	165	0.79	0.95	37	GTP, MG
5	185	0.78	0.94	39	empty

Interfaces

9 interfaces between chains.

A–E · 1611 Å² buried · 24 hydrogen bonds · protein-protein
C–D · 1524 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 1492 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 942 Å² buried · 16 hydrogen bonds · protein-protein
C–E · 824 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6Y6D · Tubulin-7-Aminonoscapine complex · the same entry in another collection · chain A against A, 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 P81947
Every structure of UniProt Q6B856
Every structure of UniProt P63043
Every structure of UniProt E1BQ43
Elsewhere: RCSB PDB 6Y6D · PDBe 6Y6D · UniProt P81947 · UniProt Q6B856 · UniProt P63043 · UniProt E1BQ43

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