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Extracellular srcr domains of human CD6

Analyse Extracellular srcr domains of human CD6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A2E
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T-cell differentiation antigen CD6
UniProt: P30203
Ligands: NAG

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T-cell differentiation antigen CD6	protein	303	13% helix, 35% strand	P30203

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
EDO · 1,2-ethanediol · additive · 6 copies · chains A

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

Modifications

Observed in the structure: 12 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

5A2E · Extracellular SRCR domains of human CD6 · the same entry in another collection · chain A against A, TM-score 1.00
P30203 · AlphaFold monomer V2.0 prediction for T-cell differentiation antigen CD6 (P30203) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P30203
Elsewhere: RCSB PDB 5A2E · PDBe 5A2E · UniProt P30203

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