5DQR
The crystal structure of Arabidopsis 7-hydroxymethyl chlorophyll a reductase (HCAR)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0009507 | cellular_component | chloroplast |
| A | 0015994 | biological_process | chlorophyll metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0033354 | biological_process | chlorophyll cycle |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0090415 | molecular_function | 7-hydroxymethyl chlorophyll a reductase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0009507 | cellular_component | chloroplast |
| B | 0015994 | biological_process | chlorophyll metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0033354 | biological_process | chlorophyll cycle |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0090415 | molecular_function | 7-hydroxymethyl chlorophyll a reductase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0009507 | cellular_component | chloroplast |
| C | 0015994 | biological_process | chlorophyll metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0033354 | biological_process | chlorophyll cycle |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0090415 | molecular_function | 7-hydroxymethyl chlorophyll a reductase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0009507 | cellular_component | chloroplast |
| D | 0015994 | biological_process | chlorophyll metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0033354 | biological_process | chlorophyll cycle |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0090415 | molecular_function | 7-hydroxymethyl chlorophyll a reductase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005576 | cellular_component | extracellular region |
| E | 0009507 | cellular_component | chloroplast |
| E | 0015994 | biological_process | chlorophyll metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0033354 | biological_process | chlorophyll cycle |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0090415 | molecular_function | 7-hydroxymethyl chlorophyll a reductase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005576 | cellular_component | extracellular region |
| F | 0009507 | cellular_component | chloroplast |
| F | 0015994 | biological_process | chlorophyll metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0033354 | biological_process | chlorophyll cycle |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0090415 | molecular_function | 7-hydroxymethyl chlorophyll a reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 A 501 |
| Chain | Residue |
| A | CYS62 |
| A | SER63 |
| A | CYS65 |
| A | LEU67 |
| A | CYS68 |
| A | CYS80 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SF4 A 502 |
| Chain | Residue |
| A | CYS302 |
| A | CYS211 |
| A | CYS235 |
| A | CYS299 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue FAD A 503 |
| Chain | Residue |
| A | ALA130 |
| A | GLN131 |
| A | TRP132 |
| A | GLY134 |
| A | ILE135 |
| A | VAL136 |
| A | THR137 |
| A | CYS154 |
| A | VAL155 |
| A | ALA179 |
| A | GLY181 |
| A | VAL182 |
| A | LYS183 |
| A | THR185 |
| A | SER187 |
| A | ASN189 |
| A | THR233 |
| A | ASN234 |
| A | CYS235 |
| A | VAL236 |
| A | ASN238 |
| A | GLU262 |
| A | TYR305 |
| A | ILE314 |
| A | GLY315 |
| A | TYR316 |
| A | MET317 |
| A | GLN332 |
| A | HOH611 |
| A | HOH658 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 B 501 |
| Chain | Residue |
| B | TYR56 |
| B | ALA58 |
| B | CYS62 |
| B | SER63 |
| B | GLN64 |
| B | CYS65 |
| B | CYS68 |
| B | CYS80 |
| B | HOH678 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 502 |
| Chain | Residue |
| B | VAL209 |
| B | GLY210 |
| B | CYS211 |
| B | CYS235 |
| B | SER298 |
| B | CYS299 |
| B | CYS302 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | binding site for residue FAD B 503 |
| Chain | Residue |
| B | ALA130 |
| B | GLN131 |
| B | TRP132 |
| B | GLY134 |
| B | ILE135 |
| B | VAL136 |
| B | THR137 |
| B | CYS154 |
| B | VAL155 |
| B | ALA179 |
| B | GLY181 |
| B | VAL182 |
| B | LYS183 |
| B | THR185 |
| B | SER187 |
| B | THR233 |
| B | ASN234 |
| B | CYS235 |
| B | VAL236 |
| B | ASN238 |
| B | GLU262 |
| B | TYR305 |
| B | ILE314 |
| B | GLY315 |
| B | TYR316 |
| B | MET317 |
| B | GLN332 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 C 501 |
| Chain | Residue |
| C | ALA58 |
| C | CYS62 |
| C | SER63 |
| C | CYS65 |
| C | CYS68 |
| C | CYS80 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SF4 C 502 |
| Chain | Residue |
| C | VAL209 |
| C | CYS211 |
| C | CYS235 |
| C | CYS299 |
| C | CYS302 |
| site_id | AC9 |
| Number of Residues | 30 |
| Details | binding site for residue FAD C 503 |
| Chain | Residue |
| C | VAL136 |
| C | THR137 |
| C | CYS154 |
| C | VAL155 |
| C | ALA179 |
| C | GLY181 |
| C | VAL182 |
| C | LYS183 |
| C | THR185 |
| C | SER187 |
| C | ASN189 |
| C | THR233 |
| C | ASN234 |
| C | CYS235 |
| C | VAL236 |
| C | ASN238 |
| C | GLU262 |
| C | TYR305 |
| C | ILE314 |
| C | GLY315 |
| C | TYR316 |
| C | MET317 |
| C | GLN332 |
| C | HOH613 |
| C | HOH625 |
| C | ALA130 |
| C | GLN131 |
| C | TRP132 |
| C | GLY134 |
| C | ILE135 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 D 501 |
| Chain | Residue |
| D | ALA58 |
| D | CYS62 |
| D | SER63 |
| D | GLN64 |
| D | CYS65 |
| D | LEU67 |
| D | CYS68 |
| D | CYS80 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SF4 D 502 |
| Chain | Residue |
| D | CYS211 |
| D | CYS235 |
| D | CYS299 |
| D | CYS302 |
| site_id | AD3 |
| Number of Residues | 30 |
| Details | binding site for residue FAD D 503 |
| Chain | Residue |
| D | ALA130 |
| D | GLN131 |
| D | TRP132 |
| D | GLY134 |
| D | ILE135 |
| D | VAL136 |
| D | THR137 |
| D | CYS154 |
| D | VAL155 |
| D | ALA179 |
| D | GLY181 |
| D | VAL182 |
| D | LYS183 |
| D | THR185 |
| D | SER187 |
| D | ASN189 |
| D | THR233 |
| D | ASN234 |
| D | CYS235 |
| D | VAL236 |
| D | ASN238 |
| D | GLU262 |
| D | TYR305 |
| D | ILE314 |
| D | GLY315 |
| D | TYR316 |
| D | MET317 |
| D | GLN332 |
| D | HOH638 |
| D | HOH715 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 E 501 |
| Chain | Residue |
| E | ALA58 |
| E | CYS62 |
| E | SER63 |
| E | GLN64 |
| E | CYS65 |
| E | CYS68 |
| E | CYS80 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue SF4 E 502 |
| Chain | Residue |
| E | VAL209 |
| E | CYS211 |
| E | CYS235 |
| E | CYS299 |
| E | CYS302 |
| site_id | AD6 |
| Number of Residues | 31 |
| Details | binding site for residue FAD E 503 |
| Chain | Residue |
| E | GLN131 |
| E | TRP132 |
| E | GLY134 |
| E | ILE135 |
| E | VAL136 |
| E | THR137 |
| E | CYS154 |
| E | VAL155 |
| E | ALA179 |
| E | GLY181 |
| E | VAL182 |
| E | LYS183 |
| E | THR185 |
| E | SER187 |
| E | ASN189 |
| E | THR233 |
| E | ASN234 |
| E | CYS235 |
| E | VAL236 |
| E | ASN238 |
| E | GLU262 |
| E | TYR305 |
| E | ILE314 |
| E | GLY315 |
| E | TYR316 |
| E | MET317 |
| E | GLN332 |
| E | HOH602 |
| E | HOH612 |
| E | HOH617 |
| E | HOH644 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 F 501 |
| Chain | Residue |
| F | ALA58 |
| F | CYS62 |
| F | SER63 |
| F | CYS65 |
| F | LEU67 |
| F | CYS68 |
| F | CYS80 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 F 502 |
| Chain | Residue |
| F | VAL209 |
| F | CYS211 |
| F | CYS235 |
| F | SER298 |
| F | CYS299 |
| F | CYS302 |
| site_id | AD9 |
| Number of Residues | 30 |
| Details | binding site for residue FAD F 503 |
| Chain | Residue |
| F | ALA130 |
| F | GLN131 |
| F | TRP132 |
| F | GLY134 |
| F | ILE135 |
| F | VAL136 |
| F | THR137 |
| F | CYS154 |
| F | VAL155 |
| F | ALA179 |
| F | GLY181 |
| F | VAL182 |
| F | LYS183 |
| F | THR185 |
| F | SER187 |
| F | ASN189 |
| F | THR233 |
| F | ASN234 |
| F | CYS235 |
| F | VAL236 |
| F | ASN238 |
| F | GLU262 |
| F | TYR305 |
| F | ILE314 |
| F | GLY315 |
| F | TYR316 |
| F | MET317 |
| F | GLN332 |
| F | HOH618 |
| F | HOH619 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 990 |
| Chain | Residue | Details |
| D | ASP237 | proton acceptor, proton donor |
| D | GLU262 | electrostatic stabiliser |
| D | GLN332 | electrostatic stabiliser |
| D | HIS417 | electrostatic stabiliser, metal ligand |
