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Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)

Analyse Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WU9
Type: protein
Length: 126 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein RP/EB family member 1
UniProt: Q15691
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Microtubule-associated protein RP/EB family member 1	protein	59	85% helix, 0% strand	Q15691
B	Microtubule-associated protein RP/EB family member 1	protein	67	82% helix, 0% strand	Q15691

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.31	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 1622 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1WU9 · Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1) · the same entry in another collection · chain A against A, TM-score 1.00
Q15691 · AlphaFold monomer V2.0 prediction for microtubule-associated protein RP/EB family member… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q15691
Elsewhere: RCSB PDB 1WU9 · PDBe 1WU9 · UniProt Q15691

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