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Structure of the TBC1D7-TSC1 complex

Analyse Structure of the TBC1D7-TSC1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Z6Y
Type: protein
Length: 1,304 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TBC1 domain family member 7; Hamartin
UniProt: Q9P0N9, Q92574
Pockets: 13 · best druggability 0.61

Structure

x-ray diffraction · 5 distinct chains · 72% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, G, E	TBC1 domain family member 7	protein	272	67% helix, 1% strand	Q9P0N9
C, D	Hamartin	protein	53	91% helix, 0% strand	Q92574
H	Hamartin	protein	55	87% helix, 0% strand	Q92574
F	Hamartin	protein	54	87% helix, 0% strand	Q92574
A	TBC1 domain family member 7	protein	273	67% helix, 1% strand	Q9P0N9

Pockets

13 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	316	0.61	0.78	42	empty
2	269	0.55	0.77	30	empty
3	241	0.51	0.75	31	empty
4	151	0.49	0.78	27	empty
5	136	0.48	0.78	21	empty

Interfaces

10 interfaces between chains.

H–D · 886 Å² buried · 3 hydrogen bonds · protein-protein
C–F · 873 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 756 Å² buried · 5 hydrogen bonds · protein-protein
B–C · 722 Å² buried · 0 hydrogen bonds · protein-protein
E–F · 718 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4Z6Y · Structure of the TBC1D7-TSC1 complex · the same entry in another collection · chain D against D, TM-score 1.00
Q9P0N9 · AlphaFold monomer V2.0 prediction for TBC1 domain family member 7 (Q9P0N9) · a predicted model of the same protein · chain B against A, TM-score 0.99
Q92574 · AlphaFold monomer V2.0 prediction for hamartin (Q92574) · a predicted model of the same protein · chain H against A, TM-score 0.62

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 Q9P0N9
Every structure of UniProt Q92574
Elsewhere: RCSB PDB 4Z6Y · PDBe 4Z6Y · UniProt Q9P0N9 · UniProt Q92574

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