Structure analysis

Crystal structure of B.licheniformis Anti-TRAP protein, an antagonist of TRAP-RNA interactions

X-ray diffraction
2.2Å resolution
Assembly composition:
homo dodecamer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dodecamer
Accessible surface area: 23890.8 Å2
Buried surface area: 27637.23 Å2
Dissociation area: 13,811.96 Å2
Dissociation energy (ΔGdiss): 157.72 kcal/mol
Dissociation entropy (TΔSdiss): 115.73 kcal/mol
Symmetry number: 12
PDBe Complex ID: PDB-CPX-179226
Assembly 2
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Multimeric state: homo dodecamer
Accessible surface area: 24138.5 Å2
Buried surface area: 27433.53 Å2
Dissociation area: 79.49 Å2
Dissociation energy (ΔGdiss): 11.2 kcal/mol
Dissociation entropy (TΔSdiss): -1.46 kcal/mol
Symmetry number: 12
PDBe Complex ID: PDB-CPX-179226
Assembly 3
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Multimeric state: homo dodecamer
Accessible surface area: 24043.99 Å2
Buried surface area: 27497.17 Å2
Dissociation area: 251.9 Å2
Dissociation energy (ΔGdiss): 33.72 kcal/mol
Dissociation entropy (TΔSdiss): -4.37 kcal/mol
Symmetry number: 12
PDBe Complex ID: PDB-CPX-179226
Assembly 4
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Multimeric state: homo dodecamer
Accessible surface area: 23925.75 Å2
Buried surface area: 27750.23 Å2
Dissociation area: 6,361.01 Å2
Dissociation energy (ΔGdiss): 76.02 kcal/mol
Dissociation entropy (TΔSdiss): 33.38 kcal/mol
Symmetry number: 12
PDBe Complex ID: PDB-CPX-179226

Macromolecules

Chains: 1, 2, 3, 4, 5, 6, 7, 8, 9, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, j, k, l, m
Length: 53 amino acids
Theoretical weight: 5.74 KDa
Source organism: Bacillus licheniformis DSM 13 = ATCC 14580
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q65NU7 (Residues: 1-53; Coverage: 100%)
Gene names: BL05022, rtpA
Pfam: Tryptophan RNA-binding attenuator protein inhibitory protein
InterPro:
CATH: Chaperone, DNAj Protein; Chain A

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