2APC
Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP-GlcNAc phosphonate
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 | UDM449 |
A | HOH492 |
A | HOH539 |
A | HOH564 |
site_id | AC2 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE UDM A 449 |
Chain | Residue |
A | ASP144 |
A | CYS145 |
A | TYR184 |
A | LYS186 |
A | ILE187 |
A | HIS190 |
A | GLU211 |
A | ASP212 |
A | ASP213 |
A | LEU269 |
A | TRP290 |
A | ASP291 |
A | GLY320 |
A | VAL321 |
A | SER322 |
A | LEU331 |
A | MN448 |
A | GOL450 |
A | HOH459 |
A | HOH482 |
A | HOH494 |
A | HOH525 |
A | HOH564 |
A | HOH644 |
A | HOH645 |
A | HOH646 |
A | HOH647 |
A | HOH648 |
A | HOH650 |
A | HOH706 |
A | HOH707 |
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 | PHE289 |
A | ASP291 |
A | ASP292 |
A | UDM449 |
A | HOH650 |
A | HOH728 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 451 |
Chain | Residue |
A | ARG131 |
A | ILE139 |
A | ILE140 |
A | SER159 |
A | ALA160 |
A | VAL161 |
A | THR162 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 452 |
Chain | Residue |
A | TYR390 |
A | GLY412 |
A | PRO435 |
A | TRP439 |
A | GLY441 |
A | TYR442 |
A | ASP443 |
A | TRP446 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 453 |
Chain | Residue |
A | GLU149 |
A | ARG189 |
A | ARG192 |
A | HOH499 |
A | HOH552 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 454 |
Chain | Residue |
A | ASP116 |
A | PRO167 |
A | HOH525 |
A | HOH541 |
A | HOH580 |
A | HOH707 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 455 |
Chain | Residue |
A | PRO235 |
A | LEU237 |
A | LEU274 |
A | ARG303 |
A | HOH486 |
A | HOH510 |
A | HOH710 |
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 |