3FWY
Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein
Replaces: 3ENDFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0015979 | biological_process | photosynthesis |
| A | 0015995 | biological_process | chlorophyll biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
| A | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| A | 0019685 | biological_process | photosynthesis, dark reaction |
| A | 0030494 | biological_process | bacteriochlorophyll biosynthetic process |
| A | 0036070 | biological_process | light-independent bacteriochlorophyll biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0015979 | biological_process | photosynthesis |
| B | 0015995 | biological_process | chlorophyll biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
| B | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| B | 0019685 | biological_process | photosynthesis, dark reaction |
| B | 0030494 | biological_process | bacteriochlorophyll biosynthetic process |
| B | 0036070 | biological_process | light-independent bacteriochlorophyll biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | SER45 |
| A | HOH321 |
| A | HOH322 |
| A | HOH324 |
| A | HOH325 |
| A | ADP501 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP A 501 |
| Chain | Residue |
| A | LYS44 |
| A | SER45 |
| A | THR46 |
| A | LYS70 |
| A | ASN211 |
| A | ARG212 |
| A | PRO235 |
| A | ASP236 |
| A | LEU237 |
| A | ILE240 |
| A | ARG244 |
| A | HOH322 |
| A | HOH324 |
| A | HOH325 |
| A | MG401 |
| A | HOH422 |
| A | HOH468 |
| A | HOH526 |
| A | HOH534 |
| A | GLY41 |
| A | ILE42 |
| A | GLY43 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | SER45 |
| B | HOH299 |
| B | HOH300 |
| B | HOH301 |
| B | HOH302 |
| B | ADP501 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 402 |
| Chain | Residue |
| A | CYS126 |
| A | GLY127 |
| A | GLY128 |
| A | CYS160 |
| B | CYS126 |
| B | GLY127 |
| B | GLY128 |
| B | CYS160 |
| B | GLY161 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP B 501 |
| Chain | Residue |
| B | GLY41 |
| B | ILE42 |
| B | GLY43 |
| B | LYS44 |
| B | SER45 |
| B | THR46 |
| B | LYS70 |
| B | ASN211 |
| B | ARG212 |
| B | PRO235 |
| B | ASP236 |
| B | LEU237 |
| B | ILE240 |
| B | ARG241 |
| B | ARG244 |
| B | HOH300 |
| B | HOH301 |
| B | HOH302 |
| B | HOH313 |
| B | MG401 |
| B | HOH414 |
| B | HOH567 |
| B | HOH603 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19006326 |
| Chain | Residue | Details |
| A | GLY41 | |
| B | LYS70 | |
| B | CYS126 | |
| B | CYS160 | |
| B | ASN211 | |
| B | PRO235 | |
| A | SER45 | |
| A | LYS70 | |
| A | CYS126 | |
| A | CYS160 | |
| A | ASN211 | |
| A | PRO235 | |
| B | GLY41 | |
| B | SER45 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| A | LYS44 | |
| A | GLY41 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| B | LYS44 | |
| B | GLY41 |
