1DEA
STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006043 | biological_process | glucosamine catabolic process |
| A | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| A | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006043 | biological_process | glucosamine catabolic process |
| B | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| B | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 267 |
| Chain | Residue |
| A | MET1 |
| A | SER151 |
| A | SER152 |
| A | ARG158 |
| A | LYS160 |
| A | HOH338 |
| A | HOH362 |
| A | HOH364 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 268 |
| Chain | Residue |
| A | GLY43 |
| A | THR44 |
| A | ARG172 |
| A | LYS208 |
| A | HOH323 |
| A | HOH348 |
| A | HOH386 |
| A | GLY42 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 267 |
| Chain | Residue |
| B | MET1 |
| B | SER151 |
| B | SER152 |
| B | ARG158 |
| B | LYS160 |
| B | HOH299 |
| B | HOH352 |
| B | HOH402 |
| B | HOH406 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 268 |
| Chain | Residue |
| B | GLY42 |
| B | GLY43 |
| B | THR44 |
| B | ARG172 |
| B | LYS208 |
| B | HOH328 |
| B | HOH332 |
| B | HOH377 |
| B | HOH395 |
Functional Information from PROSITE/UniProt
| site_id | PS01161 |
| Number of Residues | 19 |
| Details | GLC_GALNAC_ISOMERASE Glucosamine/galactosamine-6-phosphate isomerases signature. IrsyGkIhLfMgGVGnDGH |
| Chain | Residue | Details |
| A | ILE125-HIS143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; for enolization step","evidences":[{"source":"PubMed","id":"11513596","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"For ring-opening step","evidences":[{"source":"PubMed","id":"11513596","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; for ring-opening step","evidences":[{"source":"PubMed","id":"11513596","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Site: {"description":"Part of the allosteric site"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1cd5 |
| Chain | Residue | Details |
| A | HIS143 | |
| A | GLU148 | |
| A | ASP141 | |
| A | ASP72 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1cd5 |
| Chain | Residue | Details |
| B | HIS143 | |
| B | GLU148 | |
| B | ASP141 | |
| B | ASP72 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 60 |
| Chain | Residue | Details |
| A | ASP72 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP141 | activator, hydrogen bond acceptor |
| A | HIS143 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | GLU148 | activator, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 60 |
| Chain | Residue | Details |
| B | ASP72 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP141 | activator, hydrogen bond acceptor |
| B | HIS143 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | GLU148 | activator, hydrogen bond acceptor |
