2IXC
RmlC M. tuberculosis with dTDP-rhamnose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
A | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
B | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
C | 0005515 | molecular_function | protein binding |
C | 0005829 | cellular_component | cytosol |
C | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
C | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
D | 0005515 | molecular_function | protein binding |
D | 0005829 | cellular_component | cytosol |
D | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
D | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE TRH A1199 |
Chain | Residue |
A | GLN47 |
A | HOH2218 |
A | HOH2251 |
A | HOH2252 |
A | HOH2253 |
A | HOH2254 |
A | HOH2255 |
A | HOH2256 |
A | HOH2257 |
B | HIS19 |
B | ARG23 |
A | ASN49 |
B | PHE26 |
B | GLU28 |
C | GLU90 |
C | ARG181 |
A | ARG59 |
A | HIS62 |
A | LYS72 |
A | HIS119 |
A | TYR132 |
A | TYR138 |
A | ARG170 |
site_id | AC2 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE TRH B1199 |
Chain | Residue |
A | PHE26 |
A | GLU28 |
B | GLN47 |
B | ASN49 |
B | ARG59 |
B | HIS62 |
B | LYS72 |
B | HIS119 |
B | TYR132 |
B | TYR138 |
B | GLU143 |
B | ARG170 |
B | ASP171 |
B | HOH2068 |
B | HOH2220 |
B | HOH2294 |
B | HOH2295 |
B | HOH2296 |
B | HOH2297 |
B | HOH2298 |
B | HOH2299 |
B | HOH2300 |
B | HOH2301 |
B | HOH2302 |
B | HOH2303 |
B | HOH2304 |
D | GLU90 |
D | ARG181 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE TRH C1199 |
Chain | Residue |
A | GLU90 |
A | ARG181 |
C | GLN47 |
C | ASN49 |
C | ARG59 |
C | HIS62 |
C | LYS72 |
C | HIS119 |
C | TYR132 |
C | TYR138 |
C | ARG170 |
C | HOH2213 |
C | HOH2317 |
C | HOH2318 |
C | HOH2319 |
C | HOH2320 |
C | HOH2321 |
C | HOH2322 |
C | HOH2323 |
C | HOH2324 |
C | HOH2326 |
C | HOH2327 |
D | PHE26 |
D | GLU28 |
site_id | AC4 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE TRH D1199 |
Chain | Residue |
D | HOH2274 |
B | GLU90 |
B | ARG181 |
C | HIS19 |
C | ARG23 |
C | PHE26 |
C | GLU28 |
D | GLN47 |
D | ASN49 |
D | ARG59 |
D | HIS62 |
D | LYS72 |
D | HIS119 |
D | TYR132 |
D | TYR138 |
D | ARG170 |
D | HOH2265 |
D | HOH2266 |
D | HOH2267 |
D | HOH2268 |
D | HOH2269 |
D | HOH2270 |
D | HOH2271 |
D | HOH2272 |
D | HOH2273 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17046787, ECO:0007744|PDB:2IXC |
Chain | Residue | Details |
A | HIS62 | |
B | HIS62 | |
C | HIS62 | |
D | HIS62 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9HU21 |
Chain | Residue | Details |
A | TYR132 | |
B | TYR132 | |
C | TYR132 | |
D | TYR132 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXC |
Chain | Residue | Details |
A | ARG23 | |
D | ARG23 | |
D | GLU28 | |
D | ARG59 | |
A | GLU28 | |
A | ARG59 | |
B | ARG23 | |
B | GLU28 | |
B | ARG59 | |
C | ARG23 | |
C | GLU28 | |
C | ARG59 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:17046787, ECO:0007744|PDB:2IXC |
Chain | Residue | Details |
A | GLN47 | |
B | GLN47 | |
C | GLN47 | |
D | GLN47 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000305|PubMed:12951098, ECO:0007744|PDB:1PM7 |
Chain | Residue | Details |
A | LYS72 | |
B | LYS72 | |
C | LYS72 | |
D | LYS72 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000305|PubMed:12951098, ECO:0007744|PDB:1PM7, ECO:0007744|PDB:2IXC |
Chain | Residue | Details |
A | HIS119 | |
B | HIS119 | |
C | HIS119 | |
D | HIS119 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9HU21 |
Chain | Residue | Details |
A | GLU143 | |
A | ARG170 | |
B | GLU143 | |
B | ARG170 | |
C | GLU143 | |
C | ARG170 | |
D | GLU143 | |
D | ARG170 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | SITE: Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose => ECO:0000250|UniProtKB:Q5SFD1 |
Chain | Residue | Details |
A | TYR138 | |
B | TYR138 | |
C | TYR138 | |
D | TYR138 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dzr |
Chain | Residue | Details |
A | HIS62 | |
A | ASP171 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dzr |
Chain | Residue | Details |
B | HIS62 | |
B | ASP171 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dzr |
Chain | Residue | Details |
C | HIS62 | |
C | ASP171 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dzr |
Chain | Residue | Details |
D | HIS62 | |
D | ASP171 |