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Structure of human clustered protocadherin gamma B3 EC1-4

Analyse Structure of human clustered protocadherin gamma B3 EC1-4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5K8R
Type: protein
Length: 414 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protocadherin gamma-B3
UniProt: Q9Y5G1
Ligands: CA, NA, CL

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protocadherin gamma-B3	protein	414	7% helix, 46% strand	Q9Y5G1

Ligands and binding sites

CA · Calcium ion · metal · 9 copies · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5K8R · Structure of human clustered protocadherin gamma B3 EC1-4 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y5G1 · AlphaFold monomer V2.0 prediction for protocadherin gamma-B3 (Q9Y5G1) · 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 Q9Y5G1
Elsewhere: RCSB PDB 5K8R · PDBe 5K8R · UniProt Q9Y5G1

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