Structure analysis

X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA

X-ray diffraction
2.3Å resolution
Source organism: Pseudomonas aeruginosa
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6577.53 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 10
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Multimeric state: monomeric
Accessible surface area: 6564.01 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 11
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Multimeric state: monomeric
Accessible surface area: 6615.26 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 12
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Multimeric state: monomeric
Accessible surface area: 6709.14 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 6719.87 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 6566.48 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 4
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Multimeric state: monomeric
Accessible surface area: 6643.34 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 5
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Multimeric state: monomeric
Accessible surface area: 6543.29 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 6
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Multimeric state: monomeric
Accessible surface area: 6650.59 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 7
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Multimeric state: monomeric
Accessible surface area: 6669.51 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 8
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Multimeric state: monomeric
Accessible surface area: 6548.44 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372
Assembly 9
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Multimeric state: monomeric
Accessible surface area: 6546.87 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132372

Macromolecules

Chains: A, B, C, D, E, F, G, H, I, K, L, M
Length: 128 amino acids
Theoretical weight: 13.9 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P00282 (Residues: 21-148; Coverage: 100%)
Gene names: PA4922, azu
Pfam: Copper binding proteins, plastocyanin/azurin family
InterPro:
CATH: Cupredoxins - blue copper proteins
SCOP: Plastocyanin/azurin-like
PDBe-KB: UniProt Coverage View: P00282  
1128102030405060708090100110120
 
50100AECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSKLKEGEQYMSFCTFPGHSALMKGTLTLK
UniProt
P00282
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation

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