1BXK
DTDP-GLUCOSE 4,6-DEHYDRATASE FROM E. COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009225 | biological_process | nucleotide-sugar metabolic process |
| A | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0009225 | biological_process | nucleotide-sugar metabolic process |
| B | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD A 380 |
| Chain | Residue |
| A | GLY8 |
| A | ALA38 |
| A | GLY39 |
| A | VAL58 |
| A | ASP59 |
| A | ILE60 |
| A | LEU81 |
| A | ALA83 |
| A | THR100 |
| A | ILE132 |
| A | SER133 |
| A | ALA10 |
| A | THR134 |
| A | TYR160 |
| A | LYS164 |
| A | CYS187 |
| A | SER188 |
| A | ASN189 |
| A | ASN190 |
| A | HOH381 |
| A | HOH382 |
| A | HOH383 |
| A | GLY11 |
| A | HOH386 |
| A | HOH387 |
| A | HOH395 |
| A | HOH479 |
| A | HOH491 |
| A | PHE12 |
| A | ILE13 |
| A | ASP33 |
| A | LYS34 |
| A | LEU35 |
| A | THR36 |
| site_id | AC2 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD B 780 |
| Chain | Residue |
| B | HOH14 |
| B | HOH18 |
| B | HOH25 |
| B | HOH53 |
| B | HOH65 |
| B | HOH69 |
| B | HOH92 |
| B | HOH194 |
| B | HOH201 |
| B | GLY408 |
| B | ALA410 |
| B | GLY411 |
| B | PHE412 |
| B | ILE413 |
| B | ASP433 |
| B | LYS434 |
| B | LEU435 |
| B | THR436 |
| B | ALA438 |
| B | GLY439 |
| B | VAL458 |
| B | ASP459 |
| B | ILE460 |
| B | LEU481 |
| B | ALA483 |
| B | THR500 |
| B | ILE532 |
| B | SER533 |
| B | THR534 |
| B | TYR560 |
| B | LYS564 |
| B | CYS587 |
| B | SER588 |
| B | ASN590 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11380254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11601973","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11380254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11601973","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-1998","submissionDatabase":"PDB data bank","title":"Molecular structure of dTDP-glucose 4,6-dehydratase from E. coli.","authors":["Thoden J.B.","Hegeman A.D.","Frey P.A.","Holden H.M."]}},{"source":"PDB","id":"1BXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"OCT-1998","submissionDatabase":"PDB data bank","title":"Molecular structure of dTDP-glucose 4,6-dehydratase from E. coli.","authors":["Thoden J.B.","Hegeman A.D.","Frey P.A.","Holden H.M."]}},{"source":"PDB","id":"1BXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P26391","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS164 | |
| A | THR134 | |
| A | TYR160 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS564 | |
| B | TYR560 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS564 | |
| B | THR534 | |
| B | TYR560 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | GLU136 | |
| A | LYS164 | |
| A | THR134 | |
| A | TYR160 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | GLU536 | |
| B | LYS564 | |
| B | THR534 | |
| B | TYR560 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS164 | |
| A | THR134 | |
| A | ASN101 | |
| A | TYR160 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS564 | |
| B | THR534 | |
| B | TYR560 | |
| B | ASN501 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS164 | |
| A | SER157 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS564 | |
| B | SER557 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS164 | |
| A | TYR160 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 228 |
| Chain | Residue | Details |
| A | THR134 | electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
| A | ASP135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU136 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | TYR160 | attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS164 | attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 228 |
| Chain | Residue | Details |
| B | THR534 | electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
| B | ASP535 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU536 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | TYR560 | attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS564 | attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity |
