Summary for 7RXN
| Entry DOI | 10.2210/pdb7rxn/pdb |
| Descriptor | RUBREDOXIN, FE (III) ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | electron transfer(iron-sulfur protein) |
| Biological source | Desulfovibrio vulgaris |
| Cellular location | Cytoplasm: P00269 |
| Total number of polymer chains | 1 |
| Total formula weight | 5730.08 |
| Authors | Adman, E.T.,Sieker, L.C.,Jensen, L.H. (deposition date: 1990-05-11, release date: 1991-07-15, Last modification date: 2024-03-06) |
| Primary citation | Adman, E.T.,Sieker, L.C.,Jensen, L.H. Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A resolution. J.Mol.Biol., 217:337-352, 1991 Cited by PubMed Abstract: The X-ray model of rubredoxin from Desulfovibrio vulgaris has been refined against 1.5 A X-ray diffraction data collected on a diffractometer. The final model comprises 395 non-hydrogen protein atoms, and 180 solvent O atoms. The final R-value for the model with calculated H atom positions included as fixed contributions is 0.098 over all reflections greater than 2 sigma I from infinity to 1.5 A. The error in co-ordinates is estimated to be 0.08 A. The solvent model was twice redetermined during the later stages of refinement and was instrumental in its success. One sequence error has been detected and corrected (Thr21----Asp). The iron-sulfur site bond angles are distorted from true tetrahedral symmetry, as found in other rubredoxin structures. A significant deviation from tetrahedral angles is seen at C alpha atoms 9, 10, 42 and 43, interior angles of the loops binding the iron atom. The planes of two aromatic groups, Tyr4 and Trp37, are nearly parallel to, and lie under, an extended system of atoms that includes the peptide bonds preceding the first cysteine residue of each cysteine loop as well as the cysteine side-chain, the iron, and the cysteine side-chain of the opposite loop, forming a previously unrecognized extended system that may function in electron transfer. PubMed: 1992166DOI: 10.1016/0022-2836(91)90547-J PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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