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Structure of tubulin H392D mutant from odinarchaeota

Analyse Structure of tubulin H392D mutant from odinarchaeota in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DON
Type: protein
Length: 423 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin-like protein cetz
UniProt: A0A1Q9N9N5
Ligands: GTP, GDP, MG
Pockets: 5 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Tubulin-like protein cetz	protein	423	45% helix, 19% strand	A0A1Q9N9N5

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · chains B
GDP · Guanosine-5'-diphosphate · ligand · chains B
MG · Magnesium ion · metal · 2 copies · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	202	0.56	0.80	32	GTP, GDP, MG
2	109	0.44	0.78	19	empty
3	64	0.43	0.82	15	empty
4	54	0.34	0.78	12	empty
5	73	0.31	0.74	17	empty

Compared structures

7DON · Structure of tubulin H392D mutant from Odinarchaeota · the same entry in another collection · chain B against B, 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 A0A1Q9N9N5
Elsewhere: RCSB PDB 7DON · PDBe 7DON · UniProt A0A1Q9N9N5

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