1HM8
CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000902 | biological_process | cell morphogenesis |
| 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 | 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 | 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 | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1902 |
| Chain | Residue |
| A | ASN405 |
| A | ASN405 |
| A | ASN405 |
| A | HOH1130 |
| A | HOH1130 |
| A | HOH1130 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2902 |
| Chain | Residue |
| B | HOH2133 |
| B | HOH2133 |
| B | HOH2133 |
| B | ASN405 |
| B | ASN405 |
| B | ASN405 |
| site_id | AC3 |
| Number of Residues | 23 |
| 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 | LYS445 |
| A | TYR448 |
| A | HOH1107 |
| A | HOH1115 |
| A | HOH1125 |
| A | HOH1132 |
| site_id | AC4 |
| Number of Residues | 25 |
| 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 | LYS445 |
| B | TYR448 |
| B | HOH2048 |
| B | HOH2051 |
| B | HOH2058 |
| B | HOH2102 |
| B | HOH2109 |
| B | HOH2131 |
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 | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | HIS362 | |
| B | HIS362 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906 |
| Chain | Residue | Details |
| A | GLU154 | |
| A | ASN169 | |
| B | LEU8 | |
| B | GLN72 | |
| B | GLY77 | |
| B | GLY139 | |
| B | GLU154 | |
| B | ASN169 | |
| A | LEU8 | |
| A | GLN72 | |
| A | GLY77 | |
| A | GLY139 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:11118459 |
| Chain | Residue | Details |
| B | ASN227 | |
| B | ASN385 | |
| A | LYS22 | |
| A | ASN227 | |
| A | ASN385 | |
| B | LYS22 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906 |
| Chain | Residue | Details |
| A | GLY101 | |
| B | GLY101 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11124906, ECO:0007744|PDB:1G97 |
| Chain | Residue | Details |
| A | ASP102 | |
| B | ASP102 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| B | ARG332 | |
| B | LYS350 | |
| B | TYR365 | |
| B | ASN376 | |
| B | ALA379 | |
| B | SER404 | |
| B | ALA422 | |
| B | ARG439 | |
| A | ARG332 | |
| A | LYS350 | |
| A | TYR365 | |
| A | ASN376 | |
| A | ALA379 | |
| A | SER404 | |
| A | ALA422 | |
| A | ARG439 |
