1HM9
CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A AND UDP-N-ACETYLGLUCOSAMINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000902 | biological_process | cell morphogenesis |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000902 | biological_process | cell morphogenesis |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1901 |
| Chain | Residue |
| A | ASP102 |
| A | ASN227 |
| A | HOH1061 |
| A | HOH1068 |
| A | UD11500 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1902 |
| Chain | Residue |
| A | UD11500 |
| A | ARG15 |
| A | HOH1250 |
| A | HOH1251 |
| A | HOH1342 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1903 |
| Chain | Residue |
| A | ASP398 |
| A | ASP416 |
| A | HOH1223 |
| B | ASP160 |
| B | HOH2320 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1904 |
| Chain | Residue |
| A | ASN405 |
| A | ASN405 |
| A | ASN405 |
| A | HOH1254 |
| A | HOH1254 |
| A | HOH1254 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 2901 |
| Chain | Residue |
| B | ASP102 |
| B | ASN227 |
| B | HOH2250 |
| B | HOH2251 |
| B | UD12500 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 2902 |
| Chain | Residue |
| B | ARG15 |
| B | HOH2208 |
| B | HOH2216 |
| B | HOH2252 |
| B | UD12500 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 2903 |
| Chain | Residue |
| A | ASP160 |
| A | HOH1339 |
| B | ASP398 |
| B | ASP416 |
| B | HOH2326 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2904 |
| Chain | Residue |
| B | ASN405 |
| B | ASN405 |
| B | ASN405 |
| B | HOH2254 |
| B | HOH2254 |
| B | HOH2254 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ACO A 1900 |
| Chain | Residue |
| A | HIS362 |
| A | GLY378 |
| A | ALA379 |
| A | ILE382 |
| A | THR383 |
| A | VAL384 |
| A | ASN385 |
| A | TYR386 |
| A | PHE401 |
| A | GLY403 |
| A | SER404 |
| A | ILE409 |
| A | GLY421 |
| A | ALA422 |
| A | ILE437 |
| A | ARG439 |
| A | ARG441 |
| A | ILE443 |
| A | LYS445 |
| A | TYR448 |
| A | HOH1039 |
| A | HOH1049 |
| A | HOH1077 |
| A | HOH1129 |
| A | HOH1205 |
| A | HOH1259 |
| A | HOH1275 |
| site_id | BC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ACO B 2900 |
| Chain | Residue |
| B | HIS362 |
| B | GLY378 |
| B | ALA379 |
| B | ILE382 |
| B | THR383 |
| B | VAL384 |
| B | ASN385 |
| B | TYR386 |
| B | PHE401 |
| B | GLY403 |
| B | SER404 |
| B | ILE409 |
| B | GLY421 |
| B | ALA422 |
| B | ILE437 |
| B | ARG439 |
| B | ARG441 |
| B | ILE443 |
| B | LYS445 |
| B | TYR448 |
| B | HOH2053 |
| B | HOH2090 |
| B | HOH2115 |
| B | HOH2158 |
| B | HOH2172 |
| B | HOH2191 |
| B | HOH2258 |
| B | HOH2273 |
| site_id | BC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE UD1 A 1500 |
| Chain | Residue |
| A | ALA10 |
| A | GLY11 |
| A | ARG15 |
| A | LYS22 |
| A | GLN72 |
| A | GLN75 |
| A | LEU76 |
| A | GLY77 |
| A | THR78 |
| A | GLY101 |
| A | ASP102 |
| A | TYR138 |
| A | GLY139 |
| A | GLU154 |
| A | ASN169 |
| A | THR170 |
| A | TYR197 |
| A | ILE198 |
| A | THR199 |
| A | ASN227 |
| A | HOH1031 |
| A | HOH1054 |
| A | HOH1061 |
| A | HOH1062 |
| A | HOH1068 |
| A | HOH1092 |
| A | HOH1110 |
| A | HOH1251 |
| A | CA1901 |
| A | CA1902 |
| A | LEU8 |
| A | ALA9 |
| site_id | BC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE UD1 B 2500 |
| Chain | Residue |
| B | LEU8 |
| B | ALA9 |
| B | ALA10 |
| B | GLY11 |
| B | ARG15 |
| B | LYS22 |
| B | GLN72 |
| B | GLN75 |
| B | LEU76 |
| B | GLY77 |
| B | THR78 |
| B | GLY101 |
| B | ASP102 |
| B | TYR138 |
| B | GLY139 |
| B | GLU154 |
| B | ASN169 |
| B | THR170 |
| B | TYR197 |
| B | ILE198 |
| B | THR199 |
| B | ASN227 |
| B | HOH2012 |
| B | HOH2016 |
| B | HOH2033 |
| B | HOH2102 |
| B | HOH2107 |
| B | HOH2250 |
| B | HOH2251 |
| B | HOH2252 |
| B | CA2901 |
| B | CA2902 |
Functional Information from PROSITE/UniProt
| site_id | PS00101 |
| Number of Residues | 29 |
| Details | HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsnStIiapVeLGdnSlVGagStItkdV |
| Chain | Residue | Details |
| A | VAL402-VAL430 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Region: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 416 |
| Details | Region: {"description":"N-acetyltransferase","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11118459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11124906","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11118459","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11118459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11124906","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11124906","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G97","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| A | SER373 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| B | SER373 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| A | ARG15 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| B | ARG15 |
