1VL0
CRYSTAL STRUCTURE OF A DTDP-4-DEHYDRORHAMNOSE REDUCTASE, RFBD ORTHOLOG (CA_C2315) FROM CLOSTRIDIUM ACETOBUTYLICUM ATCC 824 AT 2.05 A RESOLUTION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005829 | cellular_component | cytosol |
A | 0008831 | molecular_function | dTDP-4-dehydrorhamnose reductase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
A | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005829 | cellular_component | cytosol |
B | 0008831 | molecular_function | dTDP-4-dehydrorhamnose reductase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
B | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005829 | cellular_component | cytosol |
C | 0008831 | molecular_function | dTDP-4-dehydrorhamnose reductase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
C | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAI A 300 |
Chain | Residue |
A | GLY10 |
A | ALA60 |
A | THR62 |
A | ILE99 |
A | SER100 |
A | THR101 |
A | TYR125 |
A | LYS129 |
A | THR148 |
A | TRP150 |
A | LEU151 |
A | GLN11 |
A | HOH313 |
A | HOH383 |
A | LEU12 |
A | ASP31 |
A | LEU35 |
A | ASP36 |
A | ILE37 |
A | CYS58 |
A | ALA59 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE UNL A 301 |
Chain | Residue |
A | THR207 |
A | CYS208 |
A | GLY210 |
A | ILE211 |
A | LEU251 |
A | ARG252 |
A | ASN253 |
A | HOH309 |
A | HOH324 |
A | HOH337 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAI B 300 |
Chain | Residue |
B | GLY10 |
B | GLN11 |
B | LEU12 |
B | ASP31 |
B | VAL32 |
B | LEU35 |
B | ASP36 |
B | ILE37 |
B | CYS58 |
B | ALA59 |
B | ALA60 |
B | THR62 |
B | ILE77 |
B | ILE99 |
B | SER100 |
B | THR101 |
B | TYR125 |
B | LYS129 |
B | THR148 |
B | LEU151 |
B | HOH306 |
B | HOH309 |
B | HOH349 |
B | HOH360 |
B | HOH445 |
site_id | AC4 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAI C 300 |
Chain | Residue |
C | GLY10 |
C | GLN11 |
C | LEU12 |
C | ASP31 |
C | VAL32 |
C | LEU35 |
C | ASP36 |
C | ILE37 |
C | CYS58 |
C | ALA59 |
C | ALA60 |
C | THR62 |
C | ILE99 |
C | SER100 |
C | THR101 |
C | TYR125 |
C | LYS129 |
C | THR148 |
C | TRP150 |
C | LEU151 |
C | HOH306 |
C | HOH310 |
C | HOH318 |
C | HOH394 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | TYR103 | |
A | THR101 | |
A | LYS129 | |
A | TYR125 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | GLN122 | |
A | LYS129 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
B | GLN122 | |
B | LYS129 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
C | GLN122 | |
C | LYS129 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | LYS129 | |
A | TYR125 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
B | LYS129 | |
B | TYR125 |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
C | LYS129 | |
C | TYR125 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
B | TYR103 | |
B | THR101 | |
B | LYS129 | |
B | TYR125 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
C | TYR103 | |
C | THR101 | |
C | LYS129 | |
C | TYR125 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | LYS129 | |
A | THR101 | |
A | TYR125 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
B | LYS129 | |
B | THR101 | |
B | TYR125 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
C | LYS129 | |
C | THR101 | |
C | TYR125 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | LYS129 | |
A | THR101 | |
A | TYR125 | |
A | ASN78 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
B | LYS129 | |
B | THR101 | |
B | TYR125 | |
B | ASN78 |
site_id | CSA9 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
C | LYS129 | |
C | THR101 | |
C | TYR125 | |
C | ASN78 |