MolNFT v1 · #75794 · protein

N-terminal coiled-coil dimer domain of C. reinhardtii sas-6 homolog BLD12P

3Q0X · Centriole protein: “N-terminal coiled-coil dimer domain of C. reinhardtii sas-6 homolog BLD12P”. X-ray diffraction, 4 pockets (best druggability 0.51). MolNFT v1 #75794 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3Q0X
Type: protein
Length: 408 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Centriole protein
UniProt: A9CQL4
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Centriole protein	protein	206	39% helix, 34% strand	A9CQL4
B	Centriole protein	protein	202	37% helix, 37% strand	A9CQL4

Pockets

4 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	61	0.51	0.86	22	empty
2	62	0.50	0.86	19	empty
3	103	0.41	0.76	16	empty
4	53	0.33	0.77	12	empty

Interfaces

1 interface between chains.

A–B · 1970 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3Q0X · N-terminal coiled-coil dimer domain of C. reinhardtii SAS-6 homolog Bld12p · 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 A9CQL4
Elsewhere: RCSB PDB 3Q0X · PDBe 3Q0X · UniProt A9CQL4

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