› 3ttd

X-ray diffraction
2.2Å resolution

Crystal structure of E. coli HypF with AMP-CPP and carbamoyl phosphate

Released:
DOI: 10.2210/pdb3ttd/pdb
PDB entry 3ttd coloured by chain, front view.
PDB entry 3ttd coloured by chain, side view.
PDB entry 3ttd coloured by chain, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites.
Petkun S, Shi R, Li Y, Asinas A, Munger C, Zhang L, Waclawek M, Soboh B, Sawers RG, Cygler M
Structure 19 1773-83 (2011)
PMID: 22153500

Function and Biology Details

Reaction catalysed: 
An acylphosphate + H(2)O = a carboxylate + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101901 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbamoyltransferase HypF Chain: A
Molecule details ›
Chain: A
Length: 658 amino acids
Theoretical weight: 71.23 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H3JHT3 (Residues: 92-747; Coverage: 88%)
Gene names: ECs_3568, hypF
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 3 x ZN
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 46.446Å b: 77.73Å c: 200.635Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Targeting adenylate-forming enzymes with designed sulfonyladenosine inhibitors.
Lux et al. (2019)
1 more

1 mention without citation

Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers.
Patel et al. (2018)