Structure analysis

An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance

X-ray diffraction
2Å resolution
Source organism: Escherichia coli
Assembly composition:
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 34371.1 Å2
Buried surface area: 13307.51 Å2
Dissociation area: 5,103.5 Å2
Dissociation energy (ΔGdiss): 126.62 kcal/mol
Dissociation entropy (TΔSdiss): 28.97 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-159623
    Assembly 1
Confidence : 98%
No. subunits : 3
Symmetry : C3
3DComplex & QSbio predictionx
No. subunits : 3
Symmetry : C3

Macromolecules

Chain: A
Length: 424 amino acids
Theoretical weight: 44.32 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P69681 (Residues: 23-428; Coverage: 100%)
Gene names: JW0441, amtB, b0451, ybaG
Pfam: Ammonium Transporter Family
InterPro:
CATH: Ammonium transporter AmtB like domains
PDBe-KB: UniProt Coverage View: P69681  
142450100150200250300350400
 
100200300400APAVADKADNAFMMICTALVLFMTIPGIALFYGGLIRGKNVLSMLTQVTVTFALVCILWVVYGYSLAFGEGNNFFGNINWLMLKNIELTAVMGSIYQYIHVAFQGSFACITVGLIVGALAERIRFSAVLIFVVVWLTLSYIPIAHMVWGGGLLASHGALDFAGGTVVAINAAIAGLVGAYLIGKRVGFGKEAFKPHNLPMVFTGTAILYIGWFGFNAGSAGTANEIAALAFVNTVVATAAAILGWIFGEWALRGKPSLLGACSGAIAGLVGVTPACGYIGVGGALIIGVVAGLAGLWGVTMLKRLLRVDDPCDVFGVAGVCGIVGCIMTGIFAASSLGGVGFAEGVTMGHQLLVQLESIAITIVWSGVVAFIGYKLADLTVGLRVPEEQEREGLDVNSHGENAYNADQAQQPAQADLEHHHHHH
UniProt
P69681
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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