6WH5
Mycobacterium tuberculosis pduO-type ATP:cobalamin adenosyltransferase bound to cob(II)alamin and PPPi
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0008817 | molecular_function | corrinoid adenosyltransferase activity |
| A | 0009236 | biological_process | cobalamin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0008817 | molecular_function | corrinoid adenosyltransferase activity |
| B | 0009236 | biological_process | cobalamin biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| C | 0008817 | molecular_function | corrinoid adenosyltransferase activity |
| C | 0009236 | biological_process | cobalamin biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue K A 201 |
| Chain | Residue |
| A | ASP167 |
| C | ILE8 |
| C | 3PO203 |
| C | B12205 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | ASN163 |
| A | HOH317 |
| A | HOH326 |
| C | 3PO203 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue 3PO A 203 |
| Chain | Residue |
| A | ARG11 |
| A | THR12 |
| A | GLY13 |
| A | THR17 |
| A | THR18 |
| A | LYS28 |
| A | B12204 |
| A | HOH303 |
| A | HOH307 |
| A | HOH324 |
| B | ARG137 |
| B | ASN163 |
| B | ASP167 |
| B | K201 |
| B | MG202 |
| B | HOH307 |
| B | HOH317 |
| B | HOH329 |
| A | THR10 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | binding site for residue B12 A 204 |
| Chain | Residue |
| A | VAL3 |
| A | HIS4 |
| A | LEU5 |
| A | THR6 |
| A | ARG7 |
| A | ILE8 |
| A | GLY19 |
| A | SER21 |
| A | MET23 |
| A | TYR36 |
| A | PHE71 |
| A | GLY74 |
| A | ALA75 |
| A | SER78 |
| A | PRO88 |
| A | PRO89 |
| A | LEU90 |
| A | 3PO203 |
| A | HOH337 |
| B | ARG7 |
| B | PHE117 |
| B | VAL118 |
| B | ARG133 |
| B | ARG137 |
| B | SER166 |
| B | ASP167 |
| B | PHE170 |
| B | K201 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue K B 201 |
| Chain | Residue |
| A | ILE8 |
| A | 3PO203 |
| A | B12204 |
| B | ASP167 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| A | 3PO203 |
| B | ASN163 |
| B | HOH317 |
| B | HOH329 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue 3PO B 203 |
| Chain | Residue |
| B | THR10 |
| B | ARG11 |
| B | THR12 |
| B | GLY13 |
| B | THR18 |
| B | LYS28 |
| B | HOH305 |
| B | HOH330 |
| B | HOH336 |
| C | ARG137 |
| C | ASN163 |
| C | ASP167 |
| C | K201 |
| C | MG202 |
| C | B12204 |
| C | HOH307 |
| C | HOH309 |
| C | HOH326 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue K C 201 |
| Chain | Residue |
| B | ILE8 |
| B | 3PO203 |
| C | ASP167 |
| C | B12204 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 202 |
| Chain | Residue |
| B | 3PO203 |
| C | ASN163 |
| C | HOH307 |
| C | HOH326 |
| site_id | AD1 |
| Number of Residues | 19 |
| Details | binding site for residue 3PO C 203 |
| Chain | Residue |
| C | THR12 |
| C | GLY13 |
| C | THR17 |
| C | THR18 |
| C | LYS28 |
| C | B12205 |
| C | HOH310 |
| C | HOH313 |
| C | HOH319 |
| A | ARG137 |
| A | ASN163 |
| A | ASP167 |
| A | K201 |
| A | MG202 |
| A | HOH310 |
| A | HOH317 |
| A | HOH326 |
| C | THR10 |
| C | ARG11 |
| site_id | AD2 |
| Number of Residues | 30 |
| Details | binding site for residue B12 C 204 |
| Chain | Residue |
| B | HIS4 |
| B | LEU5 |
| B | THR6 |
| B | ARG7 |
| B | ILE8 |
| B | GLY19 |
| B | SER21 |
| B | MET23 |
| B | TYR36 |
| B | PHE71 |
| B | GLY74 |
| B | ALA75 |
| B | SER78 |
| B | THR79 |
| B | PRO88 |
| B | PRO89 |
| B | LEU90 |
| B | 3PO203 |
| B | HOH330 |
| C | ARG7 |
| C | PHE117 |
| C | VAL118 |
| C | ARG133 |
| C | ARG137 |
| C | SER166 |
| C | ASP167 |
| C | PHE170 |
| C | K201 |
| C | HOH301 |
| C | HOH349 |
| site_id | AD3 |
| Number of Residues | 31 |
| Details | binding site for residue B12 C 205 |
| Chain | Residue |
| A | ARG7 |
| A | PHE117 |
| A | VAL118 |
| A | ARG133 |
| A | ARG137 |
| A | SER166 |
| A | ASP167 |
| A | PHE170 |
| A | TRP184 |
| A | K201 |
| C | VAL3 |
| C | HIS4 |
| C | LEU5 |
| C | THR6 |
| C | ARG7 |
| C | ILE8 |
| C | GLY19 |
| C | SER21 |
| C | MET23 |
| C | TYR36 |
| C | PHE71 |
| C | GLY74 |
| C | ALA75 |
| C | SER78 |
| C | THR79 |
| C | PRO88 |
| C | PRO89 |
| C | LEU90 |
| C | 3PO203 |
| C | HOH362 |
| C | HOH364 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 45 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
