3OZ2
Crystal structure of a geranylgeranyl bacteriochlorophyll reductase-like (Ta0516) from Thermoplasma acidophilum at 1.60 A resolution
Replaces: 3CGVFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006650 | biological_process | glycerophospholipid metabolic process |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| A | 0045550 | molecular_function | geranylgeranyl reductase activity |
| A | 0046467 | biological_process | membrane lipid biosynthetic process |
| A | 0046474 | biological_process | glycerophospholipid biosynthetic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD A 501 |
| Chain | Residue |
| A | GLY10 |
| A | GLY45 |
| A | GLU46 |
| A | GLY47 |
| A | ARG100 |
| A | PRO123 |
| A | ALA124 |
| A | ALA156 |
| A | ASP157 |
| A | GLY158 |
| A | GLU162 |
| A | GLY12 |
| A | PHE213 |
| A | VAL264 |
| A | GLY282 |
| A | ASP283 |
| A | GLY294 |
| A | GLY295 |
| A | ILE296 |
| A | ALA299 |
| A | OZ2502 |
| A | HOH517 |
| A | PRO13 |
| A | HOH518 |
| A | HOH524 |
| A | HOH528 |
| A | HOH622 |
| A | HOH623 |
| A | HOH628 |
| A | HOH630 |
| A | HOH687 |
| A | GLY14 |
| A | GLU33 |
| A | LYS34 |
| A | ARG35 |
| A | ARG43 |
| A | CYS44 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE OZ2 A 502 |
| Chain | Residue |
| A | SER49 |
| A | TYR209 |
| A | TRP211 |
| A | PRO290 |
| A | ILE291 |
| A | THR292 |
| A | GLY293 |
| A | LYS338 |
| A | LEU349 |
| A | ILE372 |
| A | SER373 |
| A | VAL374 |
| A | FAD501 |
| A | EDO508 |
| A | GOL515 |
| A | HOH655 |
| A | HOH805 |
| A | HOH836 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | VAL118 |
| A | TRP119 |
| A | VAL120 |
| A | HIS141 |
| A | HOH575 |
| A | HOH790 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | LYS138 |
| A | GLU312 |
| A | GLU315 |
| A | HOH616 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | GLY132 |
| A | LYS133 |
| A | VAL134 |
| A | MSE275 |
| A | HOH585 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 506 |
| Chain | Residue |
| A | TYR4 |
| A | HOH670 |
| A | HOH747 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 507 |
| Chain | Residue |
| A | ASN177 |
| A | SER227 |
| A | LYS346 |
| A | GLU347 |
| A | HOH617 |
| A | HOH785 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | ASP289 |
| A | THR292 |
| A | GLY294 |
| A | ASN298 |
| A | OZ2502 |
| A | EDO509 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 509 |
| Chain | Residue |
| A | ASN298 |
| A | VAL301 |
| A | ARG334 |
| A | LYS338 |
| A | EDO508 |
| A | HOH666 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 510 |
| Chain | Residue |
| A | ASP117 |
| A | TRP119 |
| A | HOH635 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 511 |
| Chain | Residue |
| A | HOH558 |
| A | HOH684 |
| A | HOH769 |
| A | HOH788 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 512 |
| Chain | Residue |
| A | LEU27 |
| A | HOH557 |
| A | HOH633 |
| A | HOH705 |
| A | ALA23 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 513 |
| Chain | Residue |
| A | GLY254 |
| A | LYS270 |
| A | MSE271 |
| A | HOH589 |
| A | HOH626 |
| A | HOH672 |
| A | HOH765 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 514 |
| Chain | Residue |
| A | PRO272 |
| A | THR274 |
| A | MSE275 |
| A | PRO321 |
| A | MSE324 |
| A | GLN325 |
| A | GLU328 |
| A | HOH604 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 515 |
| Chain | Residue |
| A | GLY47 |
| A | LEU48 |
| A | SER49 |
| A | VAL69 |
| A | THR197 |
| A | OZ2502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20869368","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OZ2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20869368","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3OZ2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






