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 | 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 | 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 | 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 |