5T2K
Geobacillus stearothermophilus HemQ with Manganese-Coproporphyrin III
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0006785 | biological_process | heme B biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0006785 | biological_process | heme B biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0006783 | biological_process | heme biosynthetic process |
| C | 0006785 | biological_process | heme B biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0006783 | biological_process | heme biosynthetic process |
| D | 0006785 | biological_process | heme B biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
| E | 0004601 | molecular_function | peroxidase activity |
| E | 0006783 | biological_process | heme biosynthetic process |
| E | 0006785 | biological_process | heme B biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue 76R A 301 |
| Chain | Residue |
| A | TYR113 |
| A | GLN184 |
| A | ILE186 |
| A | TRP197 |
| A | MET216 |
| A | SER222 |
| A | PHE228 |
| A | HOH402 |
| A | HOH430 |
| A | HOH466 |
| A | HOH542 |
| A | ARG130 |
| A | HOH554 |
| A | HOH572 |
| A | TYR144 |
| A | LYS148 |
| A | TRP156 |
| A | MET168 |
| A | HIS171 |
| A | GLY175 |
| A | ARG176 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue 76R B 301 |
| Chain | Residue |
| B | SER111 |
| B | TYR113 |
| B | ARG130 |
| B | TYR144 |
| B | LYS148 |
| B | TRP156 |
| B | MET168 |
| B | HIS171 |
| B | GLY175 |
| B | ARG176 |
| B | GLN184 |
| B | ILE186 |
| B | TRP197 |
| B | MET216 |
| B | SER222 |
| B | PHE228 |
| B | HOH405 |
| B | HOH426 |
| B | HOH447 |
| B | HOH451 |
| B | HOH461 |
| B | HOH525 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue 76R C 301 |
| Chain | Residue |
| C | SER111 |
| C | ARG130 |
| C | TYR144 |
| C | MET146 |
| C | LYS148 |
| C | TRP156 |
| C | MET168 |
| C | HIS171 |
| C | GLY172 |
| C | GLY175 |
| C | ARG176 |
| C | GLN184 |
| C | ILE186 |
| C | TRP197 |
| C | MET216 |
| C | SER222 |
| C | PHE228 |
| C | HOH413 |
| C | HOH452 |
| C | HOH488 |
| C | HOH508 |
| C | HOH539 |
| C | HOH581 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue 76R D 301 |
| Chain | Residue |
| D | SER111 |
| D | TYR113 |
| D | TYR144 |
| D | MET146 |
| D | LYS148 |
| D | TRP156 |
| D | MET168 |
| D | HIS171 |
| D | GLY172 |
| D | GLY175 |
| D | ARG176 |
| D | GLN184 |
| D | ILE186 |
| D | TRP197 |
| D | MET216 |
| D | SER222 |
| D | PHE228 |
| D | HOH414 |
| D | HOH431 |
| D | HOH454 |
| D | HOH485 |
| D | HOH506 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | binding site for residue 76R E 301 |
| Chain | Residue |
| E | TRP197 |
| E | MET216 |
| E | SER222 |
| E | PHE228 |
| E | HOH408 |
| E | HOH445 |
| E | HOH449 |
| E | HOH527 |
| E | HOH588 |
| E | TYR113 |
| E | ARG130 |
| E | TYR144 |
| E | LYS148 |
| E | TRP156 |
| E | MET168 |
| E | HIS171 |
| E | GLY175 |
| E | ARG176 |
| E | GLN184 |
| E | ILE186 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01442","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01442","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27936663","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01442","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27936663","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01442","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27936663","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






