MolNFT v1 · #124333 · protein

Crystal structure of the CBLN1 C1Q domain trimer

5KC5 · Cerebellin-1: “Crystal structure of the CBLN1 C1Q domain trimer”. X-ray diffraction, 1 ligand (NAG). MolNFT v1 #124333 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5KC5
Type: protein
Length: 137 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cerebellin-1
UniProt: P23435
Ligands: NAG

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cerebellin-1	protein	137	3% helix, 52% strand	P23435

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

Modifications

Observed in the structure: 1 glycan (N-glycosylation).

Compared structures

5KC5 · Crystal structure of the Cbln1 C1q domain trimer · the same entry in another collection · chain A against A, TM-score 1.00
P23435 · AlphaFold monomer V2.0 prediction for cerebellin-1 (P23435) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P23435
Elsewhere: RCSB PDB 5KC5 · PDBe 5KC5 · UniProt P23435

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