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Structure basis of inactivating cell abscission with chimera peptide 1

Analyse Structure basis of inactivating cell abscission with chimera peptide 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WUU
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; Tex-14
UniProt: Q53EZ4, Q8IWB6
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 9 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Centrosomal protein of 55 kda	protein	54	91% helix, 0% strand	Q53EZ4
B	Centrosomal protein of 55 kda	protein	50	94% helix, 0% strand	Q53EZ4
C, I, L	Tex-14	protein	14	0% helix, 0% strand	Q8IWB6
D, E	Centrosomal protein of 55 kda	protein	44	84% helix, 0% strand	Q53EZ4
F	Tex-14	protein	13	0% helix, 0% strand	Q8IWB6
G	Centrosomal protein of 55 kda	protein	46	80% helix, 0% strand	Q53EZ4
H	Centrosomal protein of 55 kda	protein	48	77% helix, 0% strand	Q53EZ4
J	Centrosomal protein of 55 kda	protein	55	89% helix, 0% strand	Q53EZ4
K	Centrosomal protein of 55 kda	protein	51	94% helix, 0% strand	Q53EZ4

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	343	0.57	0.75	35	empty
2	346	0.56	0.75	34	empty
3	104	0.39	0.75	20	empty

Interfaces

27 interfaces between chains.

G–H · 1169 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 1165 Å² buried · 8 hydrogen bonds · protein-protein
D–E · 1115 Å² buried · 6 hydrogen bonds · protein-protein
J–K · 1115 Å² buried · 7 hydrogen bonds · protein-protein
I–J · 601 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3WUU · Structure basis of inactivating cell abscission with chimera peptide 1 · 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 3WUU · PDBe 3WUU · UniProt Q53EZ4 · UniProt Q8IWB6

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