4PXQ
Crystal structure of D-glucuronyl C5-epimerase in complex with heparin hexasaccharide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000139 | cellular_component | Golgi membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0015012 | biological_process | heparan sulfate proteoglycan biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030210 | biological_process | heparin biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047464 | molecular_function | heparosan-N-sulfate-glucuronate 5-epimerase activity |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0015012 | biological_process | heparan sulfate proteoglycan biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030210 | biological_process | heparin biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047464 | molecular_function | heparosan-N-sulfate-glucuronate 5-epimerase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | MET1-VAL8 | |
| B | MET1-VAL8 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255 |
| Chain | Residue | Details |
| A | HIS9-ASN29 | |
| B | HIS9-ASN29 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1112 |
| Details | TOPO_DOM: Lumenal => ECO:0000305 |
| Chain | Residue | Details |
| A | ASN29-ASN585 | |
| B | ASN29-ASN585 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4PXQ |
| Chain | Residue | Details |
| A | ASN150 | |
| B | ASP155 | |
| B | ILE183 | |
| B | LEU398 | |
| B | SER483 | |
| B | HIS532 | |
| B | TRP544 | |
| B | ASP568 | |
| A | ASP155 | |
| A | ILE183 | |
| A | LEU398 | |
| A | SER483 | |
| A | HIS532 | |
| A | TRP544 | |
| A | ASP568 | |
| B | ASN150 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O94923 |
| Chain | Residue | Details |
| A | ALA208 | |
| A | GLU210 | |
| A | SER237 | |
| A | ASN361 | |
| B | ALA208 | |
| B | GLU210 | |
| B | SER237 | |
| B | ASN361 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | SITE: Critical for catalysis => ECO:0000269|PubMed:25568314 |
| Chain | Residue | Details |
| A | ASN150 | |
| A | VAL157 | |
| A | ASP529 | |
| A | HIS547 | |
| B | ASN150 | |
| B | VAL157 | |
| B | ASP529 | |
| B | HIS547 |
