MolNFT v1 · #165142 · protein

Structural basis of SALM3 dimerization and adhesion complex formation with the presynaptic receptor protein tyrosine phosphatases

6TL8: “Structural basis of SALM3 dimerization and adhesion complex formation with the presynaptic receptor protein…”. X-ray diffraction, 1 ligand (NAG). MolNFT v1 #165142 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6TL8
Type: protein
Length: 1,010 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P20138, Q80XU8
Ligands: NAG

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	251	—	P20138, Q80XU8
B	—	protein	253	—	P20138, Q80XU8
C	—	protein	253	—	P20138, Q80XU8
D	—	protein	253	—	P20138, Q80XU8

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains C, D

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

Compared structures

6TL8 · Structural basis of SALM3 dimerization and adhesion complex formation with the… · the same entry in another collection · chain C against C, TM-score 1.00
Q80XU8 · AlphaFold monomer V2.0 prediction for leucine-rich repeat and fibronectin type-III… · a predicted model of the same protein · chain C against A, TM-score 0.98
P20138 · AlphaFold monomer V2.0 prediction for myeloid cell surface antigen CD33 (P20138) · a predicted model of the same protein · chain C against A, TM-score 0.22

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 P20138
Every structure of UniProt Q80XU8
Elsewhere: RCSB PDB 6TL8 · PDBe 6TL8 · UniProt P20138 · UniProt Q80XU8

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