4HN0
Crystal Structure of ChmJ, a 3'-monoepimerase apoenzyme from Streptomyces bikiniensis
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 | 0016853 | molecular_function | isomerase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| 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 | 0016853 | molecular_function | isomerase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| B | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
| C | 0005829 | cellular_component | cytosol |
| C | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| C | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
| D | 0005829 | cellular_component | cytosol |
| D | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| 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 | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 201 |
| Chain | Residue |
| A | HIS17 |
| A | ASP19 |
| A | ARG21 |
| A | GLY22 |
| A | SER24 |
| B | ARG57 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 202 |
| Chain | Residue |
| A | TYR71 |
| A | HOH333 |
| A | PHE28 |
| A | ARG29 |
| A | SER32 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 203 |
| Chain | Residue |
| A | ASN47 |
| A | LYS70 |
| A | TYR130 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 204 |
| Chain | Residue |
| A | ARG95 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 205 |
| Chain | Residue |
| A | ARG57 |
| B | ARG21 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 201 |
| Chain | Residue |
| A | ARG57 |
| B | HIS17 |
| B | ASP19 |
| B | ARG21 |
| B | GLY22 |
| B | SER24 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 202 |
| Chain | Residue |
| B | GLN12 |
| B | PHE28 |
| B | ARG29 |
| B | SER32 |
| B | TYR71 |
| B | HOH329 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 203 |
| Chain | Residue |
| B | ASN47 |
| B | LYS70 |
| B | TYR130 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 204 |
| Chain | Residue |
| B | SER5 |
| B | GLU7 |
| B | HOH331 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 205 |
| Chain | Residue |
| B | MET1 |
| B | TRP10 |
| B | ALA36 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 206 |
| Chain | Residue |
| A | ARG21 |
| B | ARG57 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 201 |
| Chain | Residue |
| C | HIS17 |
| C | ASP19 |
| C | ARG21 |
| C | GLY22 |
| C | SER24 |
| D | ARG57 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 202 |
| Chain | Residue |
| C | ARG57 |
| C | HIS60 |
| D | ARG21 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 203 |
| Chain | Residue |
| C | ARG21 |
| D | ARG57 |
| D | HIS60 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 201 |
| Chain | Residue |
| C | ARG57 |
| D | HIS17 |
| D | ASP19 |
| D | ARG21 |
| D | GLY22 |
| D | ARG23 |
| D | SER24 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 202 |
| Chain | Residue |
| D | GLN12 |
| D | PHE28 |
| D | ARG29 |
| D | TYR71 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:23116432 |
| Chain | Residue | Details |
| A | HIS60 | |
| B | HIS60 | |
| C | HIS60 | |
| D | HIS60 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:23116432 |
| Chain | Residue | Details |
| A | TYR130 | |
| B | TYR130 | |
| C | TYR130 | |
| D | TYR130 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23116432, ECO:0007744|PDB:4HN1 |
| Chain | Residue | Details |
| A | ARG21 | |
| B | LYS70 | |
| B | ARG117 | |
| B | GLU141 | |
| C | ARG21 | |
| C | GLU26 | |
| C | ARG57 | |
| C | LYS70 | |
| C | ARG117 | |
| C | GLU141 | |
| D | ARG21 | |
| A | GLU26 | |
| D | GLU26 | |
| D | ARG57 | |
| D | LYS70 | |
| D | ARG117 | |
| D | GLU141 | |
| A | ARG57 | |
| A | LYS70 | |
| A | ARG117 | |
| A | GLU141 | |
| B | ARG21 | |
| B | GLU26 | |
| B | ARG57 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23116432, ECO:0007744|PDB:4HMZ, ECO:0007744|PDB:4HN1 |
| Chain | Residue | Details |
| A | GLN45 | |
| B | GLN45 | |
| C | GLN45 | |
| D | GLN45 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9HU21 |
| Chain | Residue | Details |
| A | ARG166 | |
| B | ARG166 | |
| C | ARG166 | |
| D | ARG166 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose => ECO:0000269|PubMed:23116432, ECO:0007744|PDB:4HN1 |
| Chain | Residue | Details |
| A | TYR136 | |
| B | TYR136 | |
| C | TYR136 | |
| D | TYR136 |
