1VKJ
Crystal structure of heparan sulfate 3-O-sulfotransferase isoform 1 in the presence of PAP
Replaces: 1S6TFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005796 | cellular_component | Golgi lumen |
| A | 0006024 | biological_process | glycosaminoglycan biosynthetic process |
| A | 0008146 | molecular_function | sulfotransferase activity |
| A | 0008467 | molecular_function | [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity |
| A | 0015012 | biological_process | heparan sulfate proteoglycan biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0005796 | cellular_component | Golgi lumen |
| B | 0006024 | biological_process | glycosaminoglycan biosynthetic process |
| B | 0008146 | molecular_function | sulfotransferase activity |
| B | 0008467 | molecular_function | [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity |
| B | 0015012 | biological_process | heparan sulfate proteoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| C | 0005794 | cellular_component | Golgi apparatus |
| C | 0005796 | cellular_component | Golgi lumen |
| C | 0006024 | biological_process | glycosaminoglycan biosynthetic process |
| C | 0008146 | molecular_function | sulfotransferase activity |
| C | 0008467 | molecular_function | [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity |
| C | 0015012 | biological_process | heparan sulfate proteoglycan biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | ARG72 |
| A | GLU90 |
| A | LYS123 |
| A | LYS274 |
| A | HOH633 |
| A | HOH681 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 602 |
| Chain | Residue |
| B | LYS274 |
| B | HOH700 |
| B | ARG72 |
| B | GLU90 |
| B | LYS123 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE A3P A 602 |
| Chain | Residue |
| A | LYS68 |
| A | GLY69 |
| A | GLY70 |
| A | THR71 |
| A | ARG72 |
| A | ALA73 |
| A | ARG151 |
| A | SER159 |
| A | ILE225 |
| A | PHE258 |
| A | TYR259 |
| A | LEU270 |
| A | LYS274 |
| A | GLY275 |
| A | ARG276 |
| A | HOH608 |
| A | HOH654 |
| A | HOH674 |
| A | HOH676 |
| A | HOH683 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE A3P A 603 |
| Chain | Residue |
| A | HOH636 |
| A | HOH637 |
| A | HOH638 |
| B | LYS68 |
| B | GLY69 |
| B | GLY70 |
| B | THR71 |
| B | ARG72 |
| B | ALA73 |
| B | ARG151 |
| B | SER159 |
| B | ILE225 |
| B | PHE258 |
| B | TYR259 |
| B | LEU270 |
| B | LYS274 |
| B | GLY275 |
| B | ARG276 |
| B | HIS278 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE A3P A 604 |
| Chain | Residue |
| C | LYS68 |
| C | GLY69 |
| C | GLY70 |
| C | THR71 |
| C | ARG72 |
| C | ALA73 |
| C | ARG151 |
| C | SER159 |
| C | ILE225 |
| C | PHE258 |
| C | TYR259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15060080 |
| Chain | Residue | Details |
| A | LYS68 | |
| B | LYS274 | |
| C | LYS68 | |
| C | ARG151 | |
| C | SER159 | |
| C | TYR259 | |
| C | LYS274 | |
| A | ARG151 | |
| A | SER159 | |
| A | TYR259 | |
| A | LYS274 | |
| B | LYS68 | |
| B | ARG151 | |
| B | SER159 | |
| B | TYR259 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN52 | |
| C | ASN196 | |
| C | ASN246 | |
| C | ASN253 | |
| A | ASN196 | |
| A | ASN246 | |
| A | ASN253 | |
| B | ASN52 | |
| B | ASN196 | |
| B | ASN246 | |
| B | ASN253 | |
| C | ASN52 |
