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 |