2Z86
Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047238 | molecular_function | glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity |
| A | 0050510 | molecular_function | N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047238 | molecular_function | glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity |
| B | 0050510 | molecular_function | N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047238 | molecular_function | glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity |
| C | 0050510 | molecular_function | N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047238 | molecular_function | glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity |
| D | 0050510 | molecular_function | N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 1 |
| Chain | Residue |
| A | ARG161 |
| A | ASP241 |
| A | HIS386 |
| A | HOH790 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN A 2 |
| Chain | Residue |
| A | ASP521 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN B 3 |
| Chain | Residue |
| B | ASP241 |
| B | HIS386 |
| B | HOH820 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 4 |
| Chain | Residue |
| B | HIS631 |
| B | HOH821 |
| B | HOH822 |
| B | ASP521 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN C 5 |
| Chain | Residue |
| C | ASP241 |
| C | HIS386 |
| C | HOH853 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN C 6 |
| Chain | Residue |
| C | ASP521 |
| C | HIS631 |
| C | HOH795 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN D 7 |
| Chain | Residue |
| D | ASP241 |
| D | HIS386 |
| D | HOH807 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN D 8 |
| Chain | Residue |
| D | ASP521 |
| D | HIS631 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE UDP B 1 |
| Chain | Residue |
| B | PRO157 |
| B | THR158 |
| B | TYR159 |
| B | ARG161 |
| B | ASP188 |
| B | TYR217 |
| B | LEU219 |
| B | ASP239 |
| B | CYS240 |
| B | ASP241 |
| B | HIS386 |
| B | HOH796 |
| B | HOH798 |
| B | HOH820 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UGA B 683 |
| Chain | Residue |
| B | ALA440 |
| B | TYR441 |
| B | ASP469 |
| B | ASN496 |
| B | GLY498 |
| B | ILE499 |
| B | GLN517 |
| B | ASP519 |
| B | SER520 |
| B | ASP521 |
| B | HIS581 |
| B | ALA603 |
| B | ASP605 |
| B | ARG628 |
| B | HIS631 |
| B | HOH730 |
| B | HOH822 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE UGA D 683 |
| Chain | Residue |
| D | PRO157 |
| D | THR158 |
| D | TYR159 |
| D | ARG161 |
| D | ASP188 |
| D | GLY216 |
| D | TYR217 |
| D | LEU219 |
| D | ARG223 |
| D | ASP239 |
| D | ASP241 |
| D | ARG268 |
| D | GLY335 |
| D | GLU361 |
| D | ASP362 |
| D | HIS386 |
| D | HOH775 |
| D | HOH780 |
| D | HOH787 |
| D | HOH807 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UGA D 684 |
| Chain | Residue |
| D | PRO439 |
| D | TYR441 |
| D | ASP469 |
| D | ASN496 |
| D | GLY498 |
| D | ILE499 |
| D | ALA502 |
| D | GLN517 |
| D | ASP519 |
| D | SER520 |
| D | ASP521 |
| D | HIS581 |
| D | ARG583 |
| D | ASN602 |
| D | ALA603 |
| D | ASP605 |
| D | ARG628 |
| D | HOH776 |
| D | HOH802 |
| site_id | BC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UDP C 1 |
| Chain | Residue |
| C | LEU219 |
| C | ASP239 |
| C | CYS240 |
| C | ASP241 |
| C | HIS386 |
| C | HOH819 |
| C | HOH853 |
| C | PRO157 |
| C | THR158 |
| C | TYR159 |
| C | ARG161 |
| C | ASP188 |
| C | TYR217 |
| site_id | BC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE UGA C 683 |
| Chain | Residue |
| C | PRO439 |
| C | TYR441 |
| C | ASP469 |
| C | ASN496 |
| C | GLY498 |
| C | ILE499 |
| C | ALA502 |
| C | GLN517 |
| C | ASP519 |
| C | SER520 |
| C | ASP521 |
| C | HIS581 |
| C | ASN602 |
| C | ALA603 |
| C | ASP605 |
| C | ARG628 |
| C | HIS631 |
| C | HOH787 |
| C | HOH795 |
| C | HOH811 |
| site_id | BC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE UGA A 683 |
| Chain | Residue |
| A | PRO157 |
| A | THR158 |
| A | TYR159 |
| A | ARG161 |
| A | ASP188 |
| A | GLY216 |
| A | TYR217 |
| A | LEU219 |
| A | ARG223 |
| A | ASP239 |
| A | CYS240 |
| A | ARG268 |
| A | GLU361 |
| A | ASP362 |
| A | HIS386 |
| A | HOH735 |
| site_id | BC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UGA A 684 |
| Chain | Residue |
| A | PRO439 |
| A | TYR441 |
| A | ASP469 |
| A | ASN496 |
| A | ILE499 |
| A | GLN517 |
| A | ASP519 |
| A | SER520 |
| A | HIS581 |
| A | ARG583 |
| A | ASN602 |
| A | ALA603 |
| A | ASP605 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 64 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18771653 |
| Chain | Residue | Details |
| A | PRO157 | |
| A | TYR441 | |
| A | ASP469 | |
| A | GLN517 | |
| A | ASP521 | |
| A | HIS581 | |
| A | ALA603 | |
| A | HIS631 | |
| B | PRO157 | |
| B | ARG161 | |
| B | ASP188 | |
| A | ARG161 | |
| B | TYR217 | |
| B | ARG223 | |
| B | ASP239 | |
| B | ASP241 | |
| B | GLU361 | |
| B | HIS386 | |
| B | TYR441 | |
| B | ASP469 | |
| B | GLN517 | |
| B | ASP521 | |
| A | ASP188 | |
| B | HIS581 | |
| B | ALA603 | |
| B | HIS631 | |
| C | PRO157 | |
| C | ARG161 | |
| C | ASP188 | |
| C | TYR217 | |
| C | ARG223 | |
| C | ASP239 | |
| C | ASP241 | |
| A | TYR217 | |
| C | GLU361 | |
| C | HIS386 | |
| C | TYR441 | |
| C | ASP469 | |
| C | GLN517 | |
| C | ASP521 | |
| C | HIS581 | |
| C | ALA603 | |
| C | HIS631 | |
| D | PRO157 | |
| A | ARG223 | |
| D | ARG161 | |
| D | ASP188 | |
| D | TYR217 | |
| D | ARG223 | |
| D | ASP239 | |
| D | ASP241 | |
| D | GLU361 | |
| D | HIS386 | |
| D | TYR441 | |
| D | ASP469 | |
| A | ASP239 | |
| D | GLN517 | |
| D | ASP521 | |
| D | HIS581 | |
| D | ALA603 | |
| D | HIS631 | |
| A | ASP241 | |
| A | GLU361 | |
| A | HIS386 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fr8 |
| Chain | Residue | Details |
| A | GLU361 | |
| A | ASN363 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fr8 |
| Chain | Residue | Details |
| B | GLU361 | |
| B | ASN363 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fr8 |
| Chain | Residue | Details |
| C | GLU361 | |
| C | ASN363 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fr8 |
| Chain | Residue | Details |
| D | GLU361 | |
| D | ASN363 |
