MolNFT v1 · #137895 · protein

Structure of a central domain of human CTC1

5W2L · Cst complex subunit CTC1: “Structure of a central domain of human CTC1”. X-ray diffraction, 1 ligand (HG), 1 pocket (best druggability 0.28). MolNFT v1 #137895 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5W2L
Type: protein
Length: 279 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cst complex subunit CTC1
UniProt: Q2NKJ3
Ligands: HG
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cst complex subunit CTC1	protein	139	15% helix, 38% strand	Q2NKJ3
B	Cst complex subunit CTC1	protein	140	15% helix, 38% strand	Q2NKJ3

Ligands and binding sites

HG · Mercury (II) ion · metal · 6 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.28	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 432 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5W2L · Structure of a central domain of human Ctc1 · the same entry in another collection · chain A against A, TM-score 1.00
Q2NKJ3 · AlphaFold monomer V2.0 prediction for cst complex subunit CTC1 (Q2NKJ3) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q2NKJ3
Elsewhere: RCSB PDB 5W2L · PDBe 5W2L · UniProt Q2NKJ3

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