Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0020037 | molecular_function | heme binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue DLE A 601 |
Chain | Residue |
A | SER63 |
A | TYR154 |
A | MET226 |
A | ALA308 |
A | ARG446 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 602 |
Chain | Residue |
A | ARG33 |
A | ASP34 |
A | ARG322 |
A | LEU324 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 603 |
Chain | Residue |
A | TYR124 |
A | MET127 |
A | ARG128 |
A | GLY129 |
A | ARG134 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 604 |
Chain | Residue |
A | ARG416 |
A | SER417 |
A | GLY418 |
B | ARG20 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue YT3 A 605 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue YT3 A 606 |
Chain | Residue |
A | GLU123 |
A | GLU126 |
A | ASP362 |
A | HOH740 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue E7L B 501 |
Chain | Residue |
B | SER63 |
B | TYR154 |
B | MET226 |
B | LEU284 |
B | ASP306 |
B | GLY307 |
B | ALA308 |
B | ARG446 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | ARG33 |
B | ARG322 |
B | LEU324 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
A | ARG20 |
B | ARG416 |
B | SER417 |
B | HOH616 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue YT3 B 504 |
Chain | Residue |
B | GLU123 |
B | ASP125 |
B | GLU126 |
B | ASP299 |
B | ASP321 |
Functional Information from PROSITE/UniProt
site_id | PS00191 |
Number of Residues | 8 |
Details | CYTOCHROME_B5_1 Cytochrome b5 family, heme-binding domain signature. FVREHPAG |
Chain | Residue | Details |
A | PHE429-GLY436 | |