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Crystal structure of mouse TEX101

Analyse Crystal structure of mouse TEX101 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BPS
Type: protein
Length: 358 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9JMI7
Ligands: NAG, FUC, SO4

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	178	—	Q9JMI7
B	—	protein	180	—	Q9JMI7

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, B
FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B
SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Compared structures

7BPS · Crystal structure of mouse TEX101 · the same entry in another collection · chain A against A, TM-score 1.00
Q9JMI7 · AlphaFold monomer V2.0 prediction for testis-expressed protein 101 (Q9JMI7) · a predicted model of the same protein · chain B 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 Q9JMI7
Elsewhere: RCSB PDB 7BPS · PDBe 7BPS · UniProt Q9JMI7

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