Carbohydrate sulfotransferase 11

UniProt data

UniProt name: CHSTB_HUMAN (Q9NPF2)

Gene name: CHST11

Organism: Homo sapiens (Human).

Function: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6- di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.

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

Transmembrane domains:

  1. 17-37, 21 AA, Helical; Signal-anchor for type II membrane protein. {ECO:0000255}.

Sequence: 352 AA

10 20 30 40 50 60 MKPALLEVMR MNRICRMVLA TCLGSFILVI FYFQSMLHPV MRRNPFGVDI CCRKGSRSPL 70 80 90 100 110 120 QELYNPIQLE LSNTAVLHQM RRDQVTDTCR ANSATSRKRR VLTPNDLKHL VVDEDHELIY 130 140 150 160 170 180 CYVPKVACTN WKRLMMVLTG RGKYSDPMEI PANEAHVSAN LKTLNQYSIP EINHRLKSYM 190 200 210 220 230 240 KFLFVREPFE RLVSAYRNKF TQKYNISFHK RYGTKIIKRQ RKNATQEALR KGDDVKFEEF 250 260 270 280 290 300 VAYLIDPHTQ REEPFNEHWQ TVYSLCHPCH IHYDLVGKYE TLEEDSNYVL QLAGVGSYLK 310 320 330 340 350 FPTYAKSTRT TDEMTTEFFQ NISSEHQTQL YEVYKLDFLM FNYSVPSYLK LE

CATM prediction

The sequence of CHSTB_HUMAN returned 1 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        4
 +    |    +    |    +    |		 (Å) (°) (Å) (°)  
Model 1 ICRMVLATCLGSFILVIFYFQSMLHAV 7.3 -54.9° 4.2 37.5 -11.6
Prolines* ICRMVLATCLGSFILVIFYFQSMLHPV          

* 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, 21, THR, HA A, 20, ALA, O 2.77Å
B, 24, GLY, HA1 A, 21, THR, O 2.82Å
A, 21, THR, HA B, 20, ALA, O 2.77Å
A, 24, GLY, HA1 B, 21, THR, O 2.82Å
A, 32, TYR, HH B, 32, TYR, OH 2.35Å