4HMZ
Crystal Structure of ChmJ, a 3'-monoepimerase from Streptomyces bikiniensis in complex with dTDP-quinovose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0005829 | cellular_component | cytosol |
| A | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016854 | molecular_function | racemase and epimerase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| B | 0000271 | biological_process | 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 | 0016854 | molecular_function | racemase and epimerase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| C | 0000271 | biological_process | 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 | 0016854 | molecular_function | racemase and epimerase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| D | 0000271 | biological_process | 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 | 0016854 | molecular_function | racemase and epimerase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 301 |
| Chain | Residue |
| A | PHE28 |
| A | ARG29 |
| A | SER32 |
| A | TYR71 |
| A | HOH401 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | PRO138 |
| A | GLU141 |
| A | HOH468 |
| A | THR62 |
| A | GLN68 |
| A | TYR136 |
| A | ALA137 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE 18T A 303 |
| Chain | Residue |
| A | GLN45 |
| A | ASN47 |
| A | ARG57 |
| A | HIS60 |
| A | LYS70 |
| A | ARG117 |
| A | LEU128 |
| A | TYR130 |
| A | TYR136 |
| A | GLU141 |
| A | ARG166 |
| A | HOH444 |
| A | HOH448 |
| A | HOH451 |
| A | HOH453 |
| A | HOH466 |
| A | HOH506 |
| A | HOH513 |
| B | HIS17 |
| B | ARG21 |
| B | SER24 |
| B | GLU26 |
| D | VAL15 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 18T B 301 |
| Chain | Residue |
| A | HIS17 |
| A | ARG21 |
| A | SER24 |
| A | GLU26 |
| A | HOH521 |
| B | GLN45 |
| B | ASN47 |
| B | ARG57 |
| B | HIS60 |
| B | LYS70 |
| B | ARG117 |
| B | LEU128 |
| B | TYR130 |
| B | TYR136 |
| B | GLU141 |
| B | ARG166 |
| B | HOH402 |
| B | HOH408 |
| B | HOH486 |
| B | HOH494 |
| B | HOH495 |
| C | VAL15 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| Chain | Residue |
| B | THR62 |
| B | GLN68 |
| B | TYR136 |
| B | ALA137 |
| B | GLU141 |
| B | HOH487 |
| B | HOH491 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 301 |
| Chain | Residue |
| C | HIS17 |
| C | ASP19 |
| C | GLY22 |
| C | ARG23 |
| C | SER24 |
| D | ARG57 |
| D | 18T303 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 18T C 302 |
| Chain | Residue |
| B | VAL15 |
| B | HIS17 |
| C | GLN45 |
| C | ASN47 |
| C | ARG57 |
| C | HIS60 |
| C | LYS70 |
| C | ARG117 |
| C | TYR130 |
| C | TYR136 |
| C | GLU141 |
| C | ARG166 |
| C | HOH405 |
| C | HOH440 |
| C | HOH444 |
| C | HOH471 |
| C | HOH472 |
| C | HOH477 |
| D | HIS17 |
| D | ARG21 |
| D | GLU26 |
| D | EDO302 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 303 |
| Chain | Residue |
| C | GLN12 |
| C | ARG29 |
| C | TYR71 |
| C | HOH433 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 301 |
| Chain | Residue |
| D | TYR71 |
| D | HOH451 |
| D | GLN12 |
| D | ARG29 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 302 |
| Chain | Residue |
| C | ARG57 |
| C | 18T302 |
| D | HIS17 |
| D | ASP19 |
| D | GLY22 |
| D | ARG23 |
| D | SER24 |
| site_id | BC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE 18T D 303 |
| Chain | Residue |
| A | VAL15 |
| A | HIS17 |
| C | HIS17 |
| C | ARG21 |
| C | GLU26 |
| C | EDO301 |
| C | HOH422 |
| D | GLN45 |
| D | ASN47 |
| D | ARG57 |
| D | HIS60 |
| D | LYS70 |
| D | ARG117 |
| D | TYR130 |
| D | TYR136 |
| D | GLU141 |
| D | ARG166 |
| D | HOH428 |
| D | HOH434 |
| D | HOH435 |
| D | HOH445 |
| D | HOH462 |
| D | HOH464 |
| D | HOH480 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HN1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HMZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HN1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9HU21","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose","evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HN1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
