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Crystal structure of the shark TBC1D15 gap domain

Analyse Crystal structure of the shark TBC1D15 gap domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TUB
Type: protein
Length: 1,332 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Shark TBC1D15 GTPase-activating protein
Pockets: 18 · best druggability 0.70

Structure

x-ray diffraction · 4 distinct chains · 63% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Shark TBC1D15 GTPase-activating protein	protein	335	63% helix, 1% strand	—
B	Shark TBC1D15 GTPase-activating protein	protein	334	63% helix, 1% strand	—
C	Shark TBC1D15 GTPase-activating protein	protein	330	63% helix, 1% strand	—
D	Shark TBC1D15 GTPase-activating protein	protein	333	64% helix, 1% strand	—

Pockets

18 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.70	0.89	32	empty
2	261	0.63	0.81	32	empty
3	136	0.61	0.85	23	empty
4	153	0.51	0.79	29	empty
5	177	0.48	0.77	27	empty

Interfaces

3 interfaces between chains.

A–C · 1034 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 977 Å² buried · 10 hydrogen bonds · protein-protein
B–D · 540 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5TUB · Crystal Structure of the Shark TBC1D15 GAP Domain · the same entry in another collection · chain A against A, 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
Elsewhere: RCSB PDB 5TUB · PDBe 5TUB

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