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Crystal structure of the chaetomium thermophilum SQT1 bound to the N- terminus of the ribosomal protein L10

Analyse Crystal structure of the chaetomium thermophilum SQT1 bound to the N- terminus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZOZ
Type: protein
Length: 812 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SQT1; 60S ribosomal protein L10-like protein
UniProt: G0S0R0, G0SEI1
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	SQT1	protein	394	3% helix, 46% strand	G0S0R0
Y, C	60S ribosomal protein L10-like protein	protein	12	58% helix, 0% strand	G0SEI1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1150	0.82	0.83	66	empty
2	1125	0.81	0.82	66	empty
3	276	0.61	0.80	47	empty
4	65	0.39	0.79	18	empty
5	82	0.34	0.75	18	empty

Interfaces

3 interfaces between chains.

B–C · 736 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 717 Å² buried · 10 hydrogen bonds · protein-protein
A–Y · 710 Å² buried · 22 hydrogen bonds · protein-protein

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 G0S0R0
Every structure of UniProt G0SEI1
Elsewhere: RCSB PDB 4ZOZ · PDBe 4ZOZ · UniProt G0S0R0 · UniProt G0SEI1

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