Research workbench

Cryo-EM structure of full-length MAP7 bound to the microtubule

Analyse Cryo-EM structure of full-length MAP7 bound to the microtubule in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7SGS
Type: protein
Length: 1,357 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin alpha-1B chain; Tubulin beta chain; Ensconsin
UniProt: Q2XVP4, P02554, Q14244
Ligands: GTP, GDP, MG
Pockets: 17 · best druggability 0.82

Structure

electron microscopy · 3 distinct chains · 49% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, D	Tubulin alpha-1B chain	protein	439	45% helix, 18% strand	Q2XVP4
C	Tubulin beta chain	protein	426	48% helix, 19% strand	P02554
A	Ensconsin	protein	53	96% helix, 0% strand	Q14244

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains B, C, D
GDP · Guanosine-5'-diphosphate · ligand · chains B, C
MG · Magnesium ion · metal · 2 copies · chains B, D

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

Pockets

17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	289	0.82	0.93	43	GTP, MG
2	653	0.81	0.86	90	GDP
3	848	0.75	0.79	66	empty
4	637	0.70	0.79	46	empty
5	271	0.62	0.80	36	GTP, MG

Interfaces

5 interfaces between chains.

C–D · 1852 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 1786 Å² buried · 20 hydrogen bonds · protein-protein
C–A · 724 Å² buried · 9 hydrogen bonds · protein-protein
D–A · 425 Å² buried · 2 hydrogen bonds · protein-protein
B–A · 160 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7SGS · Cryo-EM structure of full-length MAP7 bound to the microtubule · the same entry in another collection · chain B against B, TM-score 1.00
Q14244 · AlphaFold monomer V2.0 prediction for ensconsin (Q14244) · a predicted model of the same protein · chain A against A, TM-score 0.83

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 P02554
Every structure of UniProt Q14244
Elsewhere: RCSB PDB 7SGS · PDBe 7SGS · UniProt Q2XVP4 · UniProt P02554 · UniProt Q14244

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.