| Title | Crystal structure of A Putative Monooxygenase (YP_001095275.1) from Shewanella loihica PV-4 at 1.26 A resolution. To be published | | Site | JCSG | | PDB Id | | Target Id | 378300 | | Molecular Characteristics | | Source | Shewanella sp. pv-4 | | Alias Ids | TPS1723,YP_001095275.1 | Molecular Weight | 11050.00 Da. | | Residues | 98 | Isoelectric Point | 5.45 | | Sequence | msapvtlinpfkvpadkleaaieyweahrdfmaqqpgylstqlhqsidegatyqlinvaiwqseadfyq aaqkmrqalghvqveglcgnpalyrvirt | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 1 | | Resolution (Å) | 1.26 | Rfree | 0.162 | | Matthews' coefficent | 1.87 | Rfactor | 0.140 | | Waters | 110 | Solvent Content | 34.11 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
This structure is homologous to members of the
Dimeric alpha+beta barrel superfamily (d.58.4) from
SCOP, including
1lq9, which is a monooxygenase from Streptomyces coelicolor. Below is a superimposition of this protein with 1lq9. The gray regions are unaligned. The aligned regions are colored by weighted variety sequence conservation. The colors to from red, which is very conserved, to blue, which is not conserved.

According to Sciara
et al., the ligand binding residues in 1lq9 are: Tyr51, Asn62, Trp66, and Tyr72 and "Asn62 and Trp66 are conserved across the monooxygenase family, whereas
Tyr51 and Tyr72 are less well conserved, perhaps reflecting the
differences in the substrates utilized by the homologous enzymes in the
family." The equivalent residues in this protein are Leu44, Asn58, Trp62, and Phe68. Below is a close-up of Tyr51 and Asn62 from 1lq9 in green and Leu44 and Asn58 from this protein in yellow.

Below is a close-up of Trp66 and Tyr72 from 1lq9 in green and Trp62 and Phe68 from this protein in yellow.

References