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Literature summary for 1.14.99.57 extracted from
- Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis (2010), J. Mol. Biol., 395, 595-608.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Mycobacterium tuberculosis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| MhuD-diheme complex, to 1.75 A resolution, reveals two stacked hemes forming extensive contacts with residues in the active site. The solvent-exposed heme is axially liganded by His75 and is stacked planar upon the solvent-protected heme. The solvent-protected heme is coordinated by a chloride ion which is, in turn, stabilized by residue Asn7 | Mycobacterium tuberculosis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WKH3 | - |
- |
| Mycobacterium tuberculosis ATCC 25618 | P9WKH3 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| mycobacterial heme utilization, degrader | - |
Mycobacterium tuberculosis |
| Rv3592 | - |
Mycobacterium tuberculosis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | MhuD can bind heme in a 1:2 protein to heme ratio, although the MhuD-diheme complex is inactive | Mycobacterium tuberculosis |  |
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Release 2023.1 (January 2023)
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