Structure analysis

Crystal structure of SHP2_SH2-CagA EPIYA_D peptide complex

X-ray diffraction
2.6Å resolution
Assembly composition:
hetero trimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero trimer
Accessible surface area: 11913.26 Å2
Buried surface area: 2424.15 Å2
Dissociation area: 633.83 Å2
Dissociation energy (ΔGdiss): 9.04 kcal/mol
Dissociation entropy (TΔSdiss): 8.32 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-157377
Assembly 2 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 11513.59 Å2
Buried surface area: 2024.01 Å2
Dissociation area: 470.17 Å2
Dissociation energy (ΔGdiss): 8.03 kcal/mol
Dissociation entropy (TΔSdiss): 7 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-157377

Macromolecules

Chains: A, B
Length: 220 amino acids
Theoretical weight: 25.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q06124 (Residues: 1-220; Coverage: 37%)
Gene names: PTP2C, PTPN11, SHPTP2
Pfam: SH2 domain
InterPro:
CATH: SH2 domain
PDBe-KB: UniProt Coverage View: Q06124  
122020406080100120140160180200220
 
100200*TSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYY*EHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHV*IRCQELKYDVGGGERFDSLTDLVEHYKKNP*VETLGTVLQLKQPLNTTR
UniProt
Q06124
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Sequence conservation

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Chains: L, M, N, O
Length: 13 amino acids
Theoretical weight: 1.52 KDa
Source organism: Helicobacter pylori F32
Expression system: Not provided
UniProt:
  • Canonical: P55980 (Residues: 966-976; Coverage: 1%)
Gene names: HP_0547, cag26, cagA, cai
PDBe-KB: UniProt Coverage View: P55980  
11312345678910111213
 
510ASPEPI*ATIDFD
UniProt
P55980
Chains
Flexibility predictions
Interaction interfaces
Sequence conservation

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