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High resolution structure of the asymmetric R333G Hamp-Dhp mutant

X-ray diffraction
1.25Å resolution
PDB entry 3zcc coloured by chain, front view.
PDB entry 3zcc coloured by chain, side view.
PDB entry 3zcc coloured by chain, top view.
Source organisms:
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Sensor histidine kinase EnvZ, histidine kinase
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Multimeric state: homo dimer
Accessible surface area: 12234.94 Å2
Buried surface area: 4558.59 Å2
Dissociation area: 2,279.29 Å2
Dissociation energy (ΔGdiss): 44.73 kcal/mol
Dissociation entropy (TΔSdiss): 12.27 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-128062
Homo dimeric assembly 1 of PDB entry 3zcc coloured by chemically distinct molecules, front view.
Homo dimeric assembly 1 of PDB entry 3zcc coloured by chemically distinct molecules, side view.
Homo dimeric assembly 1 of PDB entry 3zcc coloured by chemically distinct molecules, top view.
    Assembly 1
Confidence : 96%
No. subunits : 2
Symmetry : C2
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3DComplex & QSbio predictionx
No. subunits : 2
Symmetry : C2
Evidence : This biological assembly agrees with the prediction of both PISA & EPPIC

Macromolecules

Sensor histidine kinase EnvZ; histidine kinase
Chains: A, B
Length: 114 amino acids
Theoretical weight: 12.75 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: O28769 (Residues: 278-327; Coverage: 15%)
  • Canonical: P0AEJ4 (Residues: 229-288; Coverage: 13%)
    • nullnull
Gene names: AF_1503, JW3367, b3404, envZ, ompB, perA, tpo
Pfam:
InterPro:
CATH: Helix Hairpins
HAMP domain-containing protein in PDB entry 3zcc, assembly 1, front view.
HAMP domain-containing protein in PDB entry 3zcc, assembly 1, side view.
HAMP domain-containing protein in PDB entry 3zcc, assembly 1, top view.
PDBe-KB: UniProt Coverage View: O28769   P0AEJ4  
1114102030405060708090100110
 
50100
UniProt
O28769
P0AEJ4
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Sequence conservation
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