1DZT
RMLC FROM SALMONELLA TYPHIMURIUM
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
A | 0009243 | biological_process | O antigen biosynthetic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
A | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
B | 0005829 | cellular_component | cytosol |
B | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
B | 0009243 | biological_process | O antigen biosynthetic process |
B | 0016853 | molecular_function | isomerase 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 | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | ARG60 |
A | HIS63 |
A | LYS73 |
A | HIS120 |
A | TYR133 |
A | HOH2165 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 302 |
Chain | Residue |
B | TYR133 |
B | ATY1000 |
B | HIS63 |
B | LYS73 |
B | HIS120 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE TPE A 1000 |
Chain | Residue |
A | LYS18 |
A | GLN48 |
A | ARG60 |
A | TYR139 |
A | SER167 |
A | LYS169 |
A | HOH2145 |
A | HOH2146 |
A | HOH3001 |
A | HOH3002 |
B | PHE20 |
B | ARG24 |
B | PHE27 |
B | GLU29 |
B | TYR139 |
B | PRO141 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ATY B 1000 |
Chain | Residue |
A | PHE27 |
A | GLU29 |
A | PRO141 |
A | SER142 |
A | HOH3004 |
B | GLN48 |
B | ASN50 |
B | HIS63 |
B | TYR133 |
B | TYR139 |
B | GLU144 |
B | SER167 |
B | LYS169 |
B | SO4302 |
B | HOH2050 |
B | HOH2117 |
B | HOH3005 |
B | HOH3006 |
B | HOH3007 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 201 |
Chain | Residue |
B | TRP99 |
B | GLY101 |
B | HOH2147 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 202 |
Chain | Residue |
A | PHE20 |
A | GLY25 |
A | SER142 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 203 |
Chain | Residue |
A | TRP99 |
A | VAL100 |
A | GLY101 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 204 |
Chain | Residue |
A | GLU81 |
A | LEU125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:10802738, ECO:0000269|PubMed:17046787, ECO:0007744|PDB:1DZR, ECO:0007744|PDB:1DZT |
Chain | Residue | Details |
A | HIS63 | |
B | HIS63 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:10802738, ECO:0000269|PubMed:17046787, ECO:0007744|PDB:1DZT |
Chain | Residue | Details |
A | TYR133 | |
B | TYR133 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9HU21 |
Chain | Residue | Details |
A | ARG24 | |
A | GLU144 | |
B | ARG24 | |
B | GLU144 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10802738, ECO:0007744|PDB:1DZT |
Chain | Residue | Details |
A | GLU29 | |
A | LYS169 | |
B | GLU29 | |
B | LYS169 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10802738, ECO:0007744|PDB:1DZT |
Chain | Residue | Details |
A | GLN48 | |
B | GLN48 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10802738, ECO:0007744|PDB:1DZR, ECO:0007744|PDB:1DZT |
Chain | Residue | Details |
A | ARG60 | |
A | LYS73 | |
A | HIS120 | |
B | ARG60 | |
B | LYS73 | |
B | HIS120 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
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 | TYR139 | |
B | TYR139 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dzr |
Chain | Residue | Details |
A | ASP170 | |
A | HIS63 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dzr |
Chain | Residue | Details |
B | ASP170 | |
B | HIS63 |