5IAT
Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - apo-BaP4H
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004656 | molecular_function | procollagen-proline 4-dioxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0031418 | molecular_function | L-ascorbic acid binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
B | 0004656 | molecular_function | procollagen-proline 4-dioxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0031418 | molecular_function | L-ascorbic acid binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | TYR130 |
A | ASN141 |
A | ARG142 |
A | TYR180 |
A | PHE181 |
A | ASN188 |
A | HOH432 |
B | LYS68 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue GOL B 301 |
Chain | Residue |
B | TYR130 |
B | ASN141 |
B | ARG142 |
B | TYR180 |
B | PHE181 |
B | GLN185 |
B | ASN188 |
B | HOH423 |
A | LYS68 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PEG B 302 |
Chain | Residue |
A | GLU37 |
B | PHE160 |
B | ASN165 |
B | SER167 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue PEG B 303 |
Chain | Residue |
B | LYS97 |
B | SER100 |
B | SER101 |
B | VAL105 |
B | HOH498 |