› 3hss

X-ray diffraction
1.9Å resolution

A higher resolution structure of Rv0554 from Mycobacterium tuberculosis complexed with malonic acid

Released:
DOI: 10.2210/pdb3hss/pdb
PDB entry 3hss coloured by chain, front view.
PDB entry 3hss coloured by chain, side view.
PDB entry 3hss coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural and functional analysis of Rv0554 from Mycobacterium tuberculosis: testing a putative role in menaquinone biosynthesis.
Johnston JM, Jiang M, Guo Z, Baker EN
Acta Crystallogr D Biol Crystallogr 66 909-17 (2010)
PMID: 20693690

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161858 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative non-heme bromoperoxidase BpoC Chains: A, B
Molecule details ›
Chains: A, B
Length: 293 amino acids
Theoretical weight: 32.25 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WNH1 (Residues: 2-262; Coverage: 100%)
Gene names: Rv0554, bpoC
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

5 bound ligands:
Ligand TRS 1 x TRS
Ligand EDO 6 x EDO
Ligand MLA 3 x MLA
Ligand NA 2 x NA
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P41212
Unit cell:
a: 100.454Å b: 100.454Å c: 135.162Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.219
Expression system: Escherichia coli

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Citations

7 citation in other articles

Systematic Survey of Serine Hydrolase Activity in Mycobacterium tuberculosis Defines Changes Associated with Persistence.
Ortega et al. (2016)
6 more

2 mentions without citation

Use of molecular and in silico bioinformatic tools to investigate pesticide binding to insect (Lepidoptera) phenoloxidases (PO): insights to toxicological aspects.
Aloui et al. (2014)
1 more