1FSL
FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE
Summary for 1FSL
| Entry DOI | 10.2210/pdb1fsl/pdb |
| Descriptor | LEGHEMOGLOBIN A, PROTOPORPHYRIN IX CONTAINING FE, NICOTINIC ACID, ... (4 entities in total) |
| Functional Keywords | heme, respiratory protein, nitrogen fixation, multigene family, oxygen transport |
| Biological source | Glycine max (soybean) |
| Total number of polymer chains | 2 |
| Total formula weight | 31999.86 |
| Authors | Ellis, P.J.,Guss, J.M.,Freeman, H.C. (deposition date: 1995-12-12, release date: 1996-06-26, Last modification date: 2024-02-07) |
| Primary citation | Ellis, P.J.,Appleby, C.A.,Guss, J.M.,Hunter, W.N.,Ollis, D.L.,Freeman, H.C. Structure of ferric soybean leghemoglobin a nicotinate at 2.3 A resolution. Acta Crystallogr.,Sect.D, 53:302-310, 1997 Cited by PubMed Abstract: Soybean leghemoglobin a is a small (16 kDa) protein facilitating the transport of O(2) to respiring N(2)-fixing bacteria at low free-O(2) tension. The crystal structure of soybean ferric leghemoglobin a nicotinate has been refined at 2.3 A resolution. The final R factor is 15.8% for 6877 reflections between 6.0 and 2.3 A. The structure of soybean leghemoglobin a (143 residues) is closely similar to that of lupin leghemoglobin II (153 residues), the proteins having 82 identical residues when the sequences are aligned. The new structure provides support for the conclusion that the unique properties of leghemoglobin arise principally from a heme pocket considerably larger and more flexible than that of myoglobin, a strongly ruffled heme group, and a proximal histidine orientation more favourable to ligand binding. PubMed: 15299933DOI: 10.1107/S0907444997000292 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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