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Crystal structure of human gamma-tubulin bound to gtpgammas

Analyse Crystal structure of human gamma-tubulin bound to gtpgammas in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Z5V
Type: protein
Length: 412 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin gamma-1 chain
UniProt: P23258
Ligands: GSP, MG
Pockets: 6 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tubulin gamma-1 chain	protein	412	42% helix, 18% strand	P23258

Ligands and binding sites

GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · chains A
MG · Magnesium ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.54	0.88	18	empty
2	187	0.52	0.78	36	MG, GSP
3	164	0.47	0.76	28	empty
4	66	0.33	0.76	15	empty
5	70	0.33	0.75	17	empty

Compared structures

1Z5V · Crystal structure of human gamma-tubulin bound to GTPgammaS · the same entry in another collection · chain A against A, TM-score 1.00
P23258 · AlphaFold monomer V2.0 prediction for tubulin gamma-1 chain (P23258) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P23258
Elsewhere: RCSB PDB 1Z5V · PDBe 1Z5V · UniProt P23258

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