MolNFT v1 · #177835 · protein

Odinarchaeota tubulin H393D mutant, in a psuedo protofilament arrangement, bound to 59% GDP, 41% phosphate

7EVH · Tubulin-like protein: “Odinarchaeota tubulin H393D mutant, in a psuedo protofilament arrangement, bound to 59% GDP, 41% phosphate”. X-ray diffraction, 2 ligands (GDP, PO4), 5 pockets (best druggability 0.57). MolNFT v1 #177835 on…

PDB: 7EVH
Type: protein
Length: 423 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin-like protein
UniProt: A0A1Q9N9N5
Ligands: GDP, PO4
Pockets: 5 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tubulin-like protein	protein	423	44% helix, 19% strand	A0A1Q9N9N5

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
PO4 · Phosphate ion · ion · chains A

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	209	0.57	0.80	33	GDP, PO4
2	107	0.39	0.76	31	empty
3	64	0.32	0.76	15	empty
4	72	0.32	0.75	14	empty
5	59	0.30	0.75	13	empty

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

7EVH · Odinarchaeota tubulin H393D mutant, in a psuedo protofilament arrangement, bound to 59%… · 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
Every structure of UniProt A0A1Q9N9N5
Elsewhere: RCSB PDB 7EVH · PDBe 7EVH · UniProt A0A1Q9N9N5

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