1HM0
CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU
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 | 3 |
Details | BINDING SITE FOR RESIDUE CA A 901 |
Chain | Residue |
A | ASN405 |
A | ASN405 |
A | ASN405 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA A 902 |
Chain | Residue |
A | ASP398 |
A | HOH952 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 901 |
Chain | Residue |
B | ASN405 |
B | ASN405 |
B | ASN405 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CA B 902 |
Chain | Residue |
B | ASP398 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 903 |
Chain | Residue |
B | HOH1048 |
B | HOH1048 |
B | HOH1048 |
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 | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
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_FI4 |
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_FI5 |
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_FI6 |
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_FI7 |
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 |