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Crystal structure of human protocadherin-15 EC2-3 V250N

Analyse Crystal structure of human protocadherin-15 EC2-3 V250N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EB5
Type: protein
Length: 457 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q96QU1
Ligands: CA

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	—	protein	229	—	Q96QU1
A	—	protein	228	—	Q96QU1

Ligands and binding sites

CA · Calcium ion · metal · 6 copies · chains B, A

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

Compared structures

6EB5 · Crystal Structure of Human Protocadherin-15 EC2-3 V250N · the same entry in another collection · chain B against B, TM-score 1.00
Q96QU1 · AlphaFold monomer V2.0 prediction for protocadherin-15 (Q96QU1) · a predicted model of the same protein · chain B against A, TM-score 0.64

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 Q96QU1
Elsewhere: RCSB PDB 6EB5 · PDBe 6EB5 · UniProt Q96QU1

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