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Apo odinarchaeota tubulin (odintubulin) H393D mutant, in a psuedo- protofilament arrangement

Analyse Apo odinarchaeota tubulin (odintubulin) H393D mutant, in a psuedo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EVG
Type: protein
Length: 426 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin-like protein
UniProt: A0A1Q9N9N5
Ligands: PO4
Pockets: 6 · best druggability 0.57

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tubulin-like protein	protein	426	45% helix, 19% strand	A0A1Q9N9N5

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

6 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	185	0.57	0.80	31	PO4
2	101	0.49	0.81	21	empty
3	100	0.39	0.76	28	empty
4	104	0.36	0.74	19	empty
5	71	0.35	0.76	15	empty

Compared structures

7EVG · Apo Odinarchaeota tubulin (OdinTubulin) H393D mutant, in a psuedo-protofilament… · 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 7EVG · PDBe 7EVG · UniProt A0A1Q9N9N5

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