5H63
Structure of Transferase mutant-C23S,C199S
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0043657 | cellular_component | host cell |
| A | 0044177 | cellular_component | host cell Golgi apparatus |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0090729 | molecular_function | toxin activity |
| A | 0106362 | molecular_function | protein-arginine N-acetylglucosaminyltransferase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0043657 | cellular_component | host cell |
| B | 0044177 | cellular_component | host cell Golgi apparatus |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0090729 | molecular_function | toxin activity |
| B | 0106362 | molecular_function | protein-arginine N-acetylglucosaminyltransferase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0035821 | biological_process | modulation of process of another organism |
| C | 0043657 | cellular_component | host cell |
| C | 0044177 | cellular_component | host cell Golgi apparatus |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0090729 | molecular_function | toxin activity |
| C | 0106362 | molecular_function | protein-arginine N-acetylglucosaminyltransferase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0035821 | biological_process | modulation of process of another organism |
| D | 0043657 | cellular_component | host cell |
| D | 0044177 | cellular_component | host cell Golgi apparatus |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0090729 | molecular_function | toxin activity |
| D | 0106362 | molecular_function | protein-arginine N-acetylglucosaminyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue UD1 A 401 |
| Chain | Residue |
| A | GLN64 |
| A | ASP239 |
| A | ALA240 |
| A | ASP241 |
| A | HIS260 |
| A | ASN272 |
| A | GLY273 |
| A | ASN338 |
| A | SER340 |
| A | SER345 |
| A | SER346 |
| A | TRP65 |
| A | TRP347 |
| A | ARG348 |
| A | MN402 |
| A | HOH525 |
| A | HOH542 |
| A | HOH577 |
| A | HOH607 |
| A | HOH617 |
| A | HOH636 |
| A | PHE66 |
| A | TYR88 |
| A | HIS200 |
| A | PHE203 |
| A | ASP204 |
| A | ARG207 |
| A | TYR237 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 402 |
| Chain | Residue |
| A | ASP241 |
| A | ASN338 |
| A | SER340 |
| A | UD1401 |
| A | HOH542 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 403 |
| Chain | Residue |
| A | ASP322 |
| A | ASP326 |
| A | HOH608 |
| D | ASN302 |
| D | HOH620 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | binding site for residue UD1 B 401 |
| Chain | Residue |
| B | GLN64 |
| B | TRP65 |
| B | PHE66 |
| B | TYR88 |
| B | HIS200 |
| B | PHE203 |
| B | ASP204 |
| B | ARG207 |
| B | TYR237 |
| B | ASP239 |
| B | ALA240 |
| B | ASP241 |
| B | HIS260 |
| B | ASN272 |
| B | GLY273 |
| B | ASN338 |
| B | SER340 |
| B | SER345 |
| B | SER346 |
| B | TRP347 |
| B | ARG348 |
| B | MN402 |
| B | HOH501 |
| B | HOH546 |
| B | HOH557 |
| B | HOH577 |
| B | HOH584 |
| B | HOH597 |
| B | HOH598 |
| B | HOH610 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 402 |
| Chain | Residue |
| B | ASP241 |
| B | ASN338 |
| B | SER340 |
| B | UD1401 |
| B | HOH557 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MN B 403 |
| Chain | Residue |
| B | ASP322 |
| B | ASP326 |
| C | ASN302 |
| C | HOH572 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | binding site for residue UD1 C 401 |
| Chain | Residue |
| C | HOH564 |
| C | HOH584 |
| B | SER164 |
| B | GLU165 |
| B | ASN266 |
| C | GLN64 |
| C | TRP65 |
| C | PHE66 |
| C | TYR88 |
| C | HIS200 |
| C | PHE203 |
| C | ASP204 |
| C | ARG207 |
| C | TYR237 |
| C | ASP239 |
| C | ALA240 |
| C | ASP241 |
| C | GLU271 |
| C | ASN272 |
| C | GLY273 |
| C | ASN338 |
| C | SER340 |
| C | MN402 |
| C | HOH542 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MN C 402 |
| Chain | Residue |
| C | ASP241 |
| C | ASN338 |
| C | SER340 |
| C | UD1401 |
| C | HOH520 |
| site_id | AC9 |
| Number of Residues | 29 |
| Details | binding site for residue UD1 D 401 |
| Chain | Residue |
| A | SER164 |
| A | GLU165 |
| A | ASN266 |
| D | GLN64 |
| D | TRP65 |
| D | PHE66 |
| D | TYR88 |
| D | HIS200 |
| D | PHE203 |
| D | ASP204 |
| D | ARG207 |
| D | TYR237 |
| D | ASP239 |
| D | ALA240 |
| D | ASP241 |
| D | HIS260 |
| D | GLU271 |
| D | ASN272 |
| D | GLY273 |
| D | ASN338 |
| D | SER340 |
| D | MN402 |
| D | HOH513 |
| D | HOH533 |
| D | HOH543 |
| D | HOH569 |
| D | HOH582 |
| D | HOH583 |
| D | HOH592 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MN D 402 |
| Chain | Residue |
| D | ASP241 |
| D | ASN338 |
| D | SER340 |
| D | UD1401 |
| D | HOH533 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P0DUJ8 |
| Chain | Residue | Details |
| A | GLU271 | |
| B | GLU271 | |
| C | GLU271 | |
| D | GLU271 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0DUJ8 |
| Chain | Residue | Details |
| B | SER340 | |
| B | SER345 | |
| C | GLN64 | |
| C | TYR88 | |
| C | TYR237 | |
| C | ASP241 | |
| C | ASN338 | |
| C | SER340 | |
| C | SER345 | |
| D | GLN64 | |
| D | TYR88 | |
| D | TYR237 | |
| D | ASP241 | |
| D | ASN338 | |
| D | SER340 | |
| D | SER345 | |
| A | GLN64 | |
| A | TYR88 | |
| A | TYR237 | |
| A | ASP241 | |
| A | ASN338 | |
| A | SER340 | |
| A | SER345 | |
| B | GLN64 | |
| B | TYR88 | |
| B | TYR237 | |
| B | ASP241 | |
| B | ASN338 |
