6FXJ
Structure of coproheme decarboxylase from Listeria monocytogenes in complex with iron 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 | 0016491 | molecular_function | oxidoreductase activity |
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 | 0016491 | molecular_function | oxidoreductase activity |
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 | 0016491 | molecular_function | oxidoreductase activity |
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 | 0016491 | molecular_function | oxidoreductase activity |
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 | 0016491 | molecular_function | oxidoreductase activity |
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 | 6 |
Details | binding site for residue NA A 301 |
Chain | Residue |
A | ILE63 |
A | LEU64 |
A | GLY65 |
A | ALA68 |
A | ASP69 |
B | GLU86 |
site_id | AC2 |
Number of Residues | 25 |
Details | binding site for residue FEC A 302 |
Chain | Residue |
A | TYR147 |
A | MET149 |
A | LYS151 |
A | TRP159 |
A | ILE171 |
A | HIS174 |
A | GLY178 |
A | ARG179 |
A | GLN187 |
A | TRP200 |
A | LEU204 |
A | ILE215 |
A | MET219 |
A | SER225 |
A | HOH402 |
A | HOH407 |
A | HOH432 |
A | HOH439 |
A | HOH451 |
A | HOH459 |
A | HOH466 |
D | HIS42 |
A | SER111 |
A | TYR113 |
A | LEU114 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue NA B 301 |
Chain | Residue |
B | ILE63 |
B | LEU64 |
B | GLY65 |
B | ALA68 |
B | ASP69 |
E | GLU86 |
site_id | AC4 |
Number of Residues | 19 |
Details | binding site for residue FEC B 302 |
Chain | Residue |
B | LEU110 |
B | SER111 |
B | ARG133 |
B | TYR147 |
B | MET149 |
B | LYS151 |
B | TRP159 |
B | ILE171 |
B | HIS174 |
B | GLY178 |
B | ARG179 |
B | GLN187 |
B | TRP200 |
B | LEU204 |
B | MET219 |
B | SER225 |
B | HOH422 |
B | HOH499 |
B | HOH546 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue POL B 303 |
Chain | Residue |
B | SER233 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue POL B 304 |
Chain | Residue |
B | ASP197 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue NA A 303 |
Chain | Residue |
A | GLU86 |
C | ILE63 |
C | LEU64 |
C | GLY65 |
C | ALA68 |
C | ASP69 |
C | HOH401 |
site_id | AC8 |
Number of Residues | 16 |
Details | binding site for residue FEC C 301 |
Chain | Residue |
C | SER111 |
C | ARG133 |
C | TYR147 |
C | MET149 |
C | LYS151 |
C | TRP159 |
C | HIS174 |
C | GLY178 |
C | GLN187 |
C | ILE189 |
C | TRP200 |
C | VAL202 |
C | ILE215 |
C | MET219 |
C | HOH407 |
C | HOH490 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue POL C 302 |
Chain | Residue |
C | TYR102 |
C | SER233 |
C | HOH501 |
C | HOH510 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue POL C 304 |
Chain | Residue |
C | GLN126 |
C | ASN127 |
C | HOH543 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue NA C 305 |
Chain | Residue |
C | THR50 |
C | ARG76 |
C | HOH507 |
C | HOH569 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue NA D 301 |
Chain | Residue |
C | GLU86 |
D | ILE63 |
D | GLY65 |
D | ALA68 |
D | ASP69 |
D | HOH408 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue POL D 303 |
Chain | Residue |
D | HOH525 |
D | THR101 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue POL D 305 |
Chain | Residue |
D | LYS67 |
D | THR101 |
D | SER233 |
D | HOH588 |
D | HOH666 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue CL D 307 |
Chain | Residue |
D | ARG179 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue NA E 301 |
Chain | Residue |
E | ILE63 |
E | LEU64 |
E | GLY65 |
E | ALA68 |
E | ASP69 |
E | HOH408 |
site_id | AD8 |
Number of Residues | 20 |
Details | binding site for residue FEC E 302 |
Chain | Residue |
E | SER111 |
E | TYR113 |
E | ARG133 |
E | TYR147 |
E | MET149 |
E | LYS151 |
E | TRP159 |
E | ILE171 |
E | HIS174 |
E | GLY178 |
E | ARG179 |
E | GLN187 |
E | TRP200 |
E | LEU204 |
E | MET219 |
E | SER225 |
E | HOH406 |
E | HOH412 |
E | HOH453 |
E | HOH543 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue POL E 303 |
Chain | Residue |
E | TYR102 |
E | SER233 |
E | HOH403 |
site_id | AE1 |
Number of Residues | 1 |
Details | binding site for residue POL E 304 |
Chain | Residue |
E | ASP197 |
site_id | AE2 |
Number of Residues | 32 |
Details | binding site for Di-peptide FEC D 302 and GLN D 187 |
Chain | Residue |
B | HIS42 |
D | SER111 |
D | TYR113 |
D | TYR147 |
D | MET149 |
D | LYS151 |
D | TRP159 |
D | ILE171 |
D | HIS174 |
D | GLY178 |
D | ARG179 |
D | VAL185 |
D | GLN186 |
D | ILE188 |
D | TRP200 |
D | THR203 |
D | LEU204 |
D | ILE215 |
D | MET219 |
D | SER225 |
D | PHE231 |
D | HOH414 |
D | HOH419 |
D | HOH420 |
D | HOH430 |
D | HOH433 |
D | HOH435 |
D | HOH438 |
D | HOH457 |
D | HOH481 |
D | HOH504 |
D | HOH607 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:31423350 |
Chain | Residue | Details |
A | TYR147 | |
B | TYR147 | |
C | TYR147 | |
D | TYR147 | |
E | TYR147 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ |
Chain | Residue | Details |
B | TYR147 | |
B | GLN187 | |
B | SER225 | |
C | ARG133 | |
C | TYR147 | |
C | GLN187 | |
C | SER225 | |
D | ARG133 | |
D | TYR147 | |
D | GLN187 | |
D | SER225 | |
E | ARG133 | |
E | TYR147 | |
E | GLN187 | |
E | SER225 | |
A | ARG133 | |
A | TYR147 | |
A | GLN187 | |
A | SER225 | |
B | ARG133 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ |
Chain | Residue | Details |
A | HIS174 | |
B | HIS174 | |
C | HIS174 | |
D | HIS174 | |
E | HIS174 |