MolNFT v1 · #29344 · protein

Crystal structure of gamma-tubulin bound to GTP

1Z5W · Tubulin gamma-1 chain: “Crystal structure of gamma-tubulin bound to GTP”. X-ray diffraction, 2 ligands (GTP, MG), 5 pockets (best druggability 0.49). MolNFT v1 #29344 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1Z5W
Type: protein
Length: 409 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubulin gamma-1 chain
UniProt: P23258
Ligands: GTP, MG
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tubulin gamma-1 chain	protein	409	45% helix, 18% strand	P23258

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · 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

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	142	0.49	0.78	30	MG, GTP
2	95	0.34	0.73	16	empty
3	73	0.31	0.74	15	empty
4	54	0.31	0.76	14	empty
5	68	0.30	0.74	16	empty

Compared structures

1Z5W · Crystal Structure of gamma-tubulin bound to GTP · 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 1Z5W · PDBe 1Z5W · UniProt P23258

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.