2AM5
Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 448 |
| Chain | Residue |
| A | ASP213 |
| A | UDP449 |
| A | HOH489 |
| A | HOH528 |
| A | HOH545 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UDP A 449 |
| Chain | Residue |
| A | ASP144 |
| A | CYS145 |
| A | LYS186 |
| A | ILE187 |
| A | HIS190 |
| A | GLU211 |
| A | ASP212 |
| A | ASP213 |
| A | GLY320 |
| A | VAL321 |
| A | SER322 |
| A | MN448 |
| A | GOL454 |
| A | HOH490 |
| A | HOH514 |
| A | HOH545 |
| A | HOH657 |
| A | HOH690 |
| A | HOH703 |
| A | HOH715 |
| A | ILE113 |
| A | ALA114 |
| A | CYS115 |
| A | ARG117 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 450 |
| Chain | Residue |
| A | ARG131 |
| A | PRO138 |
| A | ILE139 |
| A | SER159 |
| A | ALA160 |
| A | THR162 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 451 |
| Chain | Residue |
| A | TYR390 |
| A | GLY412 |
| A | GLY420 |
| A | TRP439 |
| A | GLY441 |
| A | TYR442 |
| A | ASP443 |
| A | TRP446 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 452 |
| Chain | Residue |
| A | ASP116 |
| A | PRO167 |
| A | VAL321 |
| A | HOH514 |
| A | HOH594 |
| A | HOH607 |
| A | HOH690 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 453 |
| Chain | Residue |
| A | PRO235 |
| A | LEU237 |
| A | LEU274 |
| A | ARG303 |
| A | HOH484 |
| A | HOH504 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 454 |
| Chain | Residue |
| A | TYR184 |
| A | GLU211 |
| A | UDP449 |
| A | HOH489 |
| A | HOH596 |
| A | HOH715 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11032794","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2APC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11032794","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FOA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11032794","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1foa |
| Chain | Residue | Details |
| A | ASP291 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 770 |
| Chain | Residue | Details |
| A | ASP213 | metal ligand |
| A | ASP291 | activator, proton acceptor, proton donor |






