Research workbench

Crystal structure of mouse C1QL1 globular domain

Analyse Crystal structure of mouse C1QL1 globular domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4D7Y
Type: protein
Length: 131 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C1Q-related factor
UniProt: O88992
Ligands: CD, NI, MG, CL

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 60% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C1Q-related factor	protein	131	0% helix, 60% strand	O88992

Ligands and binding sites

CD · Cadmium ion · metal · 2 copies · chains A
NI · Nickel (II) ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A

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

Compared structures

4D7Y · Crystal structure of mouse C1QL1 globular domain · the same entry in another collection · chain A against A, TM-score 1.00
O88992 · AlphaFold monomer V2.0 prediction for C1Q-related factor (O88992) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 O88992
Elsewhere: RCSB PDB 4D7Y · PDBe 4D7Y · UniProt O88992

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