| Title | Crystal structure of probable NifB protein that is involved in FeMo-Co biosynthesis TM1816 from Thermotoga maritima at 1.83 A resolution. To be published | | Site | JCSG | | PDB Id | | Target Id | 283669 | | Related PDB Ids 1t3v | | Molecular Characteristics | | Source | Thermotoga maritima msb8 | | Alias Ids | TPS1317,TM1816 | Molecular Weight | 13624.70 Da. | | Residues | 124 | Isoelectric Point | 6.18 | | Sequence | miiaipvsenrgkdspisehfgrapyfafvkvknnaiadisveenplaqdhvhgavpnfvkekgaelvi vrgigrraiaafeamgvkvikgasgtveevvnqylsgqlkdsdyevhdhhhhehh | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 1 | | Resolution (Å) | 1.83 | Rfree | 0.241 | | Matthews' coefficent | 2.20 | Rfactor | 0.207 | | Waters | 96 | Solvent Content | 43.55 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The gene TM1816 from Thermotoga maritima encodes a putative dinitrogenase iron-molybdenum cofactor PF02579. This conserved domain belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. This domain is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB) however, its function is still undetermined. The SCOP database suggests that this domain is most similar to structures within the ribonuclease H superfamily SCOP53146.
Ligand Summary
References