MolNFT v1 · #121024 · protein

Structure of the TSC2 N-terminus

5HIU · GTPase activator-like protein: “Structure of the TSC2 N-terminus”. X-ray diffraction, 11 pockets (best druggability 0.70). MolNFT v1 #121024 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5HIU
Type: protein
Length: 1,617 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase activator-like protein
UniProt: G0SFF5
Pockets: 11 · best druggability 0.70

Structure

x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase activator-like protein	protein	407	75% helix, 0% strand	G0SFF5
B	GTPase activator-like protein	protein	407	75% helix, 0% strand	G0SFF5
C	GTPase activator-like protein	protein	402	73% helix, 1% strand	G0SFF5
D	GTPase activator-like protein	protein	401	73% helix, 1% strand	G0SFF5

Pockets

11 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	932	0.70	0.75	76	empty
2	373	0.60	0.77	38	empty
3	152	0.48	0.77	20	empty
4	104	0.46	0.79	17	empty
5	139	0.44	0.76	22	empty

Interfaces

5 interfaces between chains.

A–B · 564 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 537 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 428 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 346 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 106 Å² buried · 2 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 G0SFF5
Elsewhere: RCSB PDB 5HIU · PDBe 5HIU · UniProt G0SFF5

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