1KET
The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Streptococcus suis with thymidine diphosphate bound
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016829 | molecular_function | lyase activity |
A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
A | 0045226 | biological_process | extracellular 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 | 0016829 | molecular_function | lyase activity |
B | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
B | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE TYD A 2573 |
Chain | Residue |
A | HIS87 |
A | TYR218 |
A | ARG225 |
A | ASN260 |
A | ARG284 |
A | HIS287 |
A | TYR340 |
A | HOH2615 |
A | HOH2632 |
A | HOH2635 |
A | HOH2811 |
A | ASN88 |
A | GLU127 |
A | ASN190 |
A | GLU199 |
A | PHE201 |
A | ARG204 |
A | GLN205 |
A | LYS216 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE TYD B 2574 |
Chain | Residue |
B | HIS87 |
B | ASN88 |
B | GLU127 |
B | ASN190 |
B | GLU199 |
B | PHE201 |
B | ARG204 |
B | GLN205 |
B | LYS216 |
B | LEU217 |
B | TYR218 |
B | ARG225 |
B | ASN260 |
B | ARG284 |
B | HIS287 |
B | TYR340 |
B | HOH2626 |
B | HOH2657 |
B | HOH2687 |
B | HOH2722 |
site_id | AC3 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE NAD A 1400 |
Chain | Residue |
A | ALA13 |
A | GLY14 |
A | PHE15 |
A | ILE16 |
A | ASP37 |
A | LYS38 |
A | LEU39 |
A | THR40 |
A | ALA42 |
A | GLY43 |
A | GLY61 |
A | ASP62 |
A | ILE63 |
A | TYR82 |
A | ALA84 |
A | SER86 |
A | THR101 |
A | VAL123 |
A | SER124 |
A | TYR161 |
A | LYS165 |
A | CYS188 |
A | SER189 |
A | ASN190 |
A | ASN191 |
A | HOH2575 |
A | HOH2578 |
A | HOH2579 |
A | HOH2583 |
A | HOH2587 |
A | HOH2592 |
A | HOH2599 |
A | HOH2606 |
A | HOH2660 |
A | HOH2784 |
site_id | AC4 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NAD B 1500 |
Chain | Residue |
B | HOH2578 |
B | HOH2580 |
B | HOH2581 |
B | HOH2583 |
B | HOH2587 |
B | HOH2594 |
B | HOH2596 |
B | HOH2635 |
B | HOH2669 |
B | ALA13 |
B | GLY14 |
B | PHE15 |
B | ILE16 |
B | ASP37 |
B | LYS38 |
B | LEU39 |
B | THR40 |
B | ALA42 |
B | GLY43 |
B | GLY61 |
B | ASP62 |
B | ILE63 |
B | TYR82 |
B | ALA84 |
B | SER86 |
B | THR101 |
B | VAL123 |
B | SER124 |
B | THR125 |
B | TYR161 |
B | LYS165 |
B | CYS188 |
B | SER189 |
B | ASN191 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P27830 |
Chain | Residue | Details |
A | ASP126 | |
B | ASP126 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P27830 |
Chain | Residue | Details |
A | GLU127 | |
B | GLU127 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11796113, ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET |
Chain | Residue | Details |
A | TYR161 | |
B | TYR161 |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11796113, ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET |
Chain | Residue | Details |
A | PHE15 | |
B | ASP62 | |
B | TYR82 | |
B | THR101 | |
B | ASN191 | |
B | LYS200 | |
A | ASP37 | |
A | ASP62 | |
A | TYR82 | |
A | THR101 | |
A | ASN191 | |
A | LYS200 | |
B | PHE15 | |
B | ASP37 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P26391 |
Chain | Residue | Details |
A | SER86 | |
B | SER86 |
site_id | SWS_FT_FI6 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11796113, ECO:0007744|PDB:1KET |
Chain | Residue | Details |
A | ASN88 | |
B | ASN260 | |
A | ASN190 | |
A | LYS216 | |
A | ARG225 | |
A | ASN260 | |
B | ASN88 | |
B | ASN190 | |
B | LYS216 | |
B | ARG225 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11796113, ECO:0007744|PDB:1KEP |
Chain | Residue | Details |
A | THR125 | |
B | THR125 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11796113, ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET |
Chain | Residue | Details |
A | TYR161 | |
B | TYR161 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11796113, ECO:0007744|PDB:1KET |
Chain | Residue | Details |
A | ASP283 | |
B | ASP283 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | TYR161 | |
A | LYS165 | |
A | THR125 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
B | TYR161 | |
B | LYS165 | |
B | THR125 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | TYR161 | |
A | GLU127 | |
A | THR125 | |
A | LYS165 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
B | TYR161 | |
B | GLU127 | |
B | THR125 | |
B | LYS165 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | TYR161 | |
A | LYS165 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
B | TYR161 | |
B | LYS165 |