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Galnac-T2 soaked with udp-sugar

Analyse Galnac-T2 soaked with udp-sugar in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NQT
Type: protein
Length: 2,943 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q10471
Ligands: LR7, MN

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	—	protein	495	—	Q10471
B	—	protein	494	—	Q10471
C	—	protein	491	—	Q10471
E	—	protein	485	—	Q10471
F	—	protein	483	—	Q10471

Ligands and binding sites

LR7 · [[(2~{R},3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene) pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{R},4~{R},5~{R},6~{R})-3-(hex-5-ynoylamino)-6-(hydroxymethyl)-4,5-bis(oxidanyl)oxan-2-yl] hydrogen phosphate · ligand · 6 copies · chains A, B, C, D, E, F
MN · Manganese (II) ion · metal · 6 copies · chains A, B, C, D, E, F

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

Compared structures

6NQT · GalNac-T2 soaked with UDP-sugar · the same entry in another collection · chain F against F, TM-score 1.00
Q10471 · AlphaFold monomer V2.0 prediction for polypeptide N-acetylgalactosaminyltransferase 2… · a predicted model of the same protein · chain C against A, TM-score 0.96

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 Q10471
Elsewhere: RCSB PDB 6NQT · PDBe 6NQT · UniProt Q10471

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