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Structure basis of inactivating cell abscission

Analyse Structure basis of inactivating cell abscission in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WUT
Type: protein
Length: 447 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Centrosomal protein of 55 kda; Inactive SERINE/THREONINE-protein kinase TEX14
UniProt: Q53EZ4, Q8IWB6
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 8 distinct chains · 88% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Centrosomal protein of 55 kda	protein	53	94% helix, 0% strand	Q53EZ4
B, J	Centrosomal protein of 55 kda	protein	44	91% helix, 0% strand	Q53EZ4
C, F, I, L	Inactive SERINE/THREONINE-protein kinase TEX14	protein	13	0% helix, 0% strand	Q8IWB6
D	Centrosomal protein of 55 kda	protein	54	93% helix, 0% strand	Q53EZ4
E	Centrosomal protein of 55 kda	protein	52	90% helix, 0% strand	Q53EZ4
G	Centrosomal protein of 55 kda	protein	55	91% helix, 0% strand	Q53EZ4
H	Centrosomal protein of 55 kda	protein	50	94% helix, 0% strand	Q53EZ4
K	Centrosomal protein of 55 kda	protein	43	86% helix, 0% strand	Q53EZ4

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B, G, H, I, D, E, F

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	178	0.47	0.75	24	GOL
2	147	0.42	0.75	21	empty
3	51	0.34	0.79	16	empty

Interfaces

26 interfaces between chains.

A–B · 1188 Å² buried · 10 hydrogen bonds · protein-protein
J–K · 1153 Å² buried · 9 hydrogen bonds · protein-protein
G–H · 1121 Å² buried · 8 hydrogen bonds · protein-protein
D–E · 1118 Å² buried · 8 hydrogen bonds · protein-protein
D–F · 577 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3WUT · Structure basis of inactivating cell abscission · the same entry in another collection · chain L against L, 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 Q53EZ4
Every structure of UniProt Q8IWB6
Elsewhere: RCSB PDB 3WUT · PDBe 3WUT · UniProt Q53EZ4 · UniProt Q8IWB6

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