1RFE image
Deposition Date 2003-11-08
Release Date 2004-12-28
Last Version Date 2025-03-26
Entry Detail
PDB ID:
1RFE
Title:
Crystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
2.00 Å
R-Value Free:
0.28
R-Value Work:
0.20
R-Value Observed:
0.20
Space Group:
P 43 2 2
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:hypothetical protein Rv2991
Gene (Uniprot):Rv2991
Chain IDs:A
Chain Length:162
Number of Molecules:1
Biological Source:Mycobacterium tuberculosis
Modified Residue
Compound ID Chain ID Parent Comp ID Details 2D Image
CSX A CYS S-OXY CYSTEINE
MSE A MET SELENOMETHIONINE
Primary Citation
The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F420binding protein with unknown function.
J. Struct. Biol. ? ? ? (2019)
PMID: 30890426 DOI: 10.1016/j.jsb.2019.03.006

Abstact

The crystal structure of the conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis has been solved by SAD using seleno-methionine substituted protein. The dimeric biological assembly and the sequence and fold conservation are typical of F420 cofactor binding enzymes. Despite Rv2991 still being of unknown function, sequence and structural comparison with similar proteins enable a role to be proposed for its C-terminal stretch of residues in recognizing and orienting the substrate. In addition, the C-terminus is involved in both protein folding and determining the size of the active site cavity.

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Disease

Primary Citation of related structures
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