Research workbench

444 in complex with tubulin

Analyse 444 in complex with tubulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DBD
Type: protein
Length: 2,190 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin alpha-1B chain; Tubulin beta chain; Stathmin-4; Tubulin tyrosine ligase
UniProt: Q2XVP4, A0A287AGU7, P63042, E1BQ43
Ligands: GTP, H0U, GDP, ACP, MG, CA
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 6 distinct chains · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tubulin alpha-1B chain	protein	438	45% helix, 19% strand	Q2XVP4
B	Tubulin beta chain	protein	429	48% helix, 19% strand	A0A287AGU7
C	Tubulin alpha-1B chain	protein	441	45% helix, 17% strand	Q2XVP4
D	Tubulin beta chain	protein	420	48% helix, 20% strand	A0A287AGU7
E	Stathmin-4	protein	123	76% helix, 13% strand	P63042
F	Tubulin tyrosine ligase	protein	339	34% helix, 22% strand	E1BQ43

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B, C, D
H0U · ~{N}-[5-(5-cyanothiophen-2-yl)-2-methyl-phenyl]-4-methyl-benzenesulfonamide · ligand · 2 copies · chains A, B, C, D
GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains B, D
ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains F
MG · Magnesium ion · metal · 4 copies · chains A, B, C, D, F
CA · Calcium ion · metal · 2 copies · chains A, C
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, 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, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	741	0.86	0.89	99	GTP, MG, H0U
2	1126	0.83	0.84	124	GTP, MG, H0U
3	780	0.81	0.84	97	MG, GDP
4	161	0.77	0.94	32	empty
5	323	0.75	0.86	40	ACP, MG

Interfaces

9 interfaces between chains.

A–E · 1644 Å² buried · 23 hydrogen bonds · protein-protein
C–D · 1452 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 1433 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 883 Å² buried · 13 hydrogen bonds · protein-protein
C–E · 803 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7DBD · 444 in complex with tubulin · the same entry in another collection · chain C against C, TM-score 1.00
P63042 · AlphaFold monomer V2.0 prediction for stathmin-4 (P63042) · a predicted model of the same protein · chain E against A, TM-score 0.77

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 Q2XVP4
Every structure of UniProt A0A287AGU7
Every structure of UniProt P63042
Every structure of UniProt E1BQ43
Elsewhere: RCSB PDB 7DBD · PDBe 7DBD · UniProt Q2XVP4 · UniProt A0A287AGU7 · UniProt P63042 · UniProt E1BQ43

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