4HN1
Crystal Structure of H60N/Y130F double mutant of ChmJ, a 3'-monoepimerase from Streptomyces bikiniensis in complex with dTDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0017000 | biological_process | antibiotic 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 | THR62 |
| A | TYR136 |
| A | ALA137 |
| A | PRO138 |
| A | HOH473 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | ARG23 |
| A | SER24 |
| B | ARG57 |
| B | TYD304 |
| A | HIS17 |
| A | ASP19 |
| A | ARG21 |
| A | GLY22 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | GLN12 |
| A | PHE28 |
| A | ARG29 |
| A | SER32 |
| A | TYR71 |
| A | HOH401 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | MET1 |
| A | TRP10 |
| A | ALA36 |
| A | HOH518 |
| D | ASN169 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TYD A 305 |
| Chain | Residue |
| A | GLN45 |
| A | ARG57 |
| A | TYR136 |
| A | HOH450 |
| A | HOH486 |
| A | HOH487 |
| A | HOH509 |
| B | HIS17 |
| B | ARG21 |
| B | GLU26 |
| B | EDO301 |
| B | HOH512 |
| D | VAL15 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE THM A 306 |
| Chain | Residue |
| A | ARG95 |
| A | TRP96 |
| A | HOH415 |
| A | HOH525 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 301 |
| Chain | Residue |
| A | ARG57 |
| A | TYD305 |
| B | HIS17 |
| B | ASP19 |
| B | ARG21 |
| B | GLY22 |
| B | SER24 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| Chain | Residue |
| B | GLN12 |
| B | PHE28 |
| B | ARG29 |
| B | SER32 |
| B | TYR71 |
| B | HOH414 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| B | THR62 |
| B | GLN68 |
| B | TYR136 |
| B | ALA137 |
| B | PRO138 |
| B | HOH467 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TYD B 304 |
| Chain | Residue |
| A | HIS17 |
| A | ARG21 |
| A | GLU26 |
| A | EDO302 |
| A | HOH503 |
| B | GLN45 |
| B | ARG57 |
| B | TYR136 |
| B | ARG166 |
| B | HOH448 |
| B | HOH493 |
| B | HOH506 |
| C | VAL15 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE THM B 305 |
| Chain | Residue |
| B | ARG95 |
| B | TRP96 |
| B | HOH423 |
| B | HOH487 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 301 |
| Chain | Residue |
| C | HIS17 |
| C | ASP19 |
| C | GLY22 |
| C | SER24 |
| C | TYD303 |
| D | ARG57 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 302 |
| Chain | Residue |
| C | GLN12 |
| C | PHE28 |
| C | ARG29 |
| C | PHE33 |
| C | TYR71 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TYD C 303 |
| Chain | Residue |
| D | ARG166 |
| D | HOH428 |
| A | VAL15 |
| A | HIS17 |
| C | HIS17 |
| C | ARG21 |
| C | GLU26 |
| C | EDO301 |
| C | HOH424 |
| C | HOH428 |
| D | GLN45 |
| D | ARG57 |
| D | TYR136 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TYD C 304 |
| Chain | Residue |
| B | VAL15 |
| B | HIS17 |
| C | GLN45 |
| C | ARG57 |
| C | TYR136 |
| C | ARG166 |
| C | HOH438 |
| C | HOH441 |
| C | HOH442 |
| D | HIS17 |
| D | ARG21 |
| D | GLU26 |
| D | EDO302 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TDR C 305 |
| Chain | Residue |
| C | ARG95 |
| C | TRP96 |
| C | HOH475 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 301 |
| Chain | Residue |
| D | GLN12 |
| D | PHE28 |
| D | ARG29 |
| D | SER32 |
| D | PHE33 |
| D | TYR71 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 302 |
| Chain | Residue |
| C | ARG57 |
| C | TYD304 |
| D | HIS17 |
| D | ASP19 |
| D | ARG21 |
| D | GLY22 |
| D | SER24 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TDR D 303 |
| Chain | Residue |
| D | ARG95 |
| D | TRP96 |
| D | HOH437 |
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 | ASN60 | |
| B | ASN60 | |
| C | ASN60 | |
| D | ASN60 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:23116432 |
| Chain | Residue | Details |
| A | PHE130 | |
| B | PHE130 | |
| C | PHE130 | |
| D | PHE130 |
| 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 |
