Galactosylceramide sulfotransferase

UniProt data

UniProt name: G3ST1_HUMAN (Q99999)

Gene name: GAL3ST1; Synonyms=CST

Organism: Homo sapiens (Human).

Function: Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes (By similarity). Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro). {ECO:0000250, ECO:0000269|PubMed:8830034}.

Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.

Transmembrane domains:

  1. 15-35, 21 AA, Helical; Signal-anchor for type II membrane protein. {ECO:0000255}.

Sequence: 423 AA

10 20 30 40 50 60 MLPPQKKPWE SMAKGLVLGA LFTSFLLLVY SYAVPPLHAG LASTTPEAAA SCSPPALEPE 70 80 90 100 110 120 AVIRANGSAG ECQPRRNIVF LKTHKTASST LLNILFRFGQ KHRLKFAFPN GRNDFDYPTF 130 140 150 160 170 180 FARSLVQDYR PGACFNIICN HMRFHYDEVR GLVPTNAIFI TVLRDPARLF ESSFHYFGPV 190 200 210 220 230 240 VPLTWKLSAG DKLTEFLQDP DRYYDPNGFN AHYLRNLLFF DLGYDNSLDP SSPQVQEHIL 250 260 270 280 290 300 EVERRFHLVL LQEYFDESLV LLKDLLCWEL EDVLYFKLNA RRDSPVPRLS GELYGRATAW 310 320 330 340 350 360 NMLDSHLYRH FNASFWRKVE AFGRERMARE VAALRHANER MRTICIDGGH AVDAAAIQDE 370 380 390 400 410 420 AMQPWQPLGT KSILGYNLKK SIGQRHAQLC RRMLTPEIQY LMDLGANLWV TKLWKFIRDF LRW

CATM prediction

The sequence of G3ST1_HUMAN returned 2 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
          20        30       
   +    |    +    |    +   
(Å) (°) (Å) (°)  
MAKGLVLGALFTSFLLLVYSYAVAALH 6.8 -54.8° 1.6 59.9 -28.5
MAKGLVLGALFTSFLLLVYSYAVAALH 7.1 -38.0° 5.7 34.0 -19.6
MAKGLVLGALFTSFLLLVYSYAVPPLH          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 16, LEU, HA A, 15, GLY, O 2.84Å
B, 19, GLY, HA1 A, 16, LEU, O 2.64Å
B, 20, ALA, HA A, 23, THR, OG1 2.38Å
A, 16, LEU, HA B, 15, GLY, O 2.84Å
A, 19, GLY, HA1 B, 16, LEU, O 2.64Å
A, 20, ALA, HA B, 23, THR, OG1 2.38Å