1F6D
THE STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE FROM E. COLI.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| A | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| B | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0000271 | biological_process | polysaccharide biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| C | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0000271 | biological_process | polysaccharide biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| D | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1378 |
| Chain | Residue |
| A | PRO298 |
| A | SER350 |
| A | ALA352 |
| A | HOH1389 |
| A | HOH1412 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1379 |
| Chain | Residue |
| A | HIS353 |
| A | ASN354 |
| A | HOH1384 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 2378 |
| Chain | Residue |
| B | SER350 |
| B | ALA352 |
| B | HOH2402 |
| B | HOH2487 |
| B | PRO298 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 2379 |
| Chain | Residue |
| B | GLY119 |
| B | ARG121 |
| B | ARG135 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 3378 |
| Chain | Residue |
| C | PRO298 |
| C | MSE349 |
| C | SER350 |
| C | ALA352 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 3379 |
| Chain | Residue |
| C | GLY119 |
| C | ARG121 |
| C | ARG135 |
| C | HOH3388 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 4378 |
| Chain | Residue |
| D | PRO298 |
| D | GLY301 |
| D | SER350 |
| D | ALA352 |
| D | HOH4386 |
| D | HOH4418 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 4379 |
| Chain | Residue |
| D | ASN354 |
| D | HOH4383 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE UDP A 1377 |
| Chain | Residue |
| A | ARG10 |
| A | ILE14 |
| A | GLN271 |
| A | TYR273 |
| A | PHE276 |
| A | GLY292 |
| A | GLU296 |
| A | HOH1567 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE UDP B 2377 |
| Chain | Residue |
| B | ARG10 |
| B | PRO11 |
| B | ILE14 |
| B | HIS213 |
| B | GLN271 |
| B | TYR273 |
| B | PHE276 |
| B | SER290 |
| B | GLY291 |
| B | GLY292 |
| B | GLU296 |
| B | HOH2385 |
| B | HOH2435 |
| B | HOH2455 |
| B | HOH2483 |
| B | HOH2532 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UDP C 3377 |
| Chain | Residue |
| C | ARG10 |
| C | PRO11 |
| C | ILE14 |
| C | HIS213 |
| C | GLN271 |
| C | TYR273 |
| C | PHE276 |
| C | SER290 |
| C | GLY291 |
| C | GLY292 |
| C | GLU296 |
| C | HOH3387 |
| C | HOH3497 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UDP D 4377 |
| Chain | Residue |
| D | ARG10 |
| D | ILE14 |
| D | GLN271 |
| D | TYR273 |
| D | PHE276 |
| D | GLY292 |
| D | GLU296 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11106477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16021622","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16021622","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 1110647, 18188181, 15518580 |
| Chain | Residue | Details |
| A | HIS213 | |
| A | ARG215 | |
| A | ASP95 | |
| A | GLU117 | |
| A | GLU131 | |
| A | HIS246 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 544 |
| Chain | Residue | Details |
| A | ILE111 | electrostatic stabiliser, proton acceptor |
| A | ALA133 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | SER147 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | ILE241 | proton shuttle (general acid/base) |
| A | TYR243 | electrostatic stabiliser |
| A | LEU274 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 544 |
| Chain | Residue | Details |
| B | ILE111 | electrostatic stabiliser, proton acceptor |
| B | ALA133 | electrostatic stabiliser, proton shuttle (general acid/base) |
| B | SER147 | electrostatic stabiliser, proton shuttle (general acid/base) |
| B | ILE241 | proton shuttle (general acid/base) |
| B | TYR243 | electrostatic stabiliser |
| B | LEU274 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 544 |
| Chain | Residue | Details |
| C | ILE111 | electrostatic stabiliser, proton acceptor |
| C | ALA133 | electrostatic stabiliser, proton shuttle (general acid/base) |
| C | SER147 | electrostatic stabiliser, proton shuttle (general acid/base) |
| C | ILE241 | proton shuttle (general acid/base) |
| C | TYR243 | electrostatic stabiliser |
| C | LEU274 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 544 |
| Chain | Residue | Details |
| D | ILE111 | electrostatic stabiliser, proton acceptor |
| D | ALA133 | electrostatic stabiliser, proton shuttle (general acid/base) |
| D | SER147 | electrostatic stabiliser, proton shuttle (general acid/base) |
| D | ILE241 | proton shuttle (general acid/base) |
| D | TYR243 | electrostatic stabiliser |
| D | LEU274 | electrostatic stabiliser |
