Structure analysis

PSEUDOMONAS LIPASE OPEN CONFORMATION

X-ray diffraction
2.1Å resolution
Source organism: Burkholderia cepacia
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 13012.78 Å2
Buried surface area: 89.88 Å2
Dissociation area: 44.94 Å2
Dissociation energy (ΔGdiss): 12.78 kcal/mol
Dissociation entropy (TΔSdiss): 0.05 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-149521

Macromolecules

Chain: A
Length: 320 amino acids
Theoretical weight: 33.15 KDa
Source organism: Burkholderia cepacia
UniProt:
  • Canonical: P22088 (Residues: 45-364; Coverage: 100%)
Gene names: lip, lipA
Pfam: alpha/beta hydrolase fold
InterPro:
CATH: alpha/beta hydrolase
SCOP: Bacterial lipase
PDBe-KB: UniProt Coverage View: P22088  
132050100150200250300
 
100200300ADNYAATRYPIILVHGLTGTDKYAGVLEYWYGIQEDLQQRGATVYVANLSGFQSDDGPNGRGEQLLAYVKTVLAATGATKVNLVGHSQGGLTSRYVAAVAPDLVASVTTIGTPHRGSEFADFVQGVLAYDPTGLSSTVIAAFVNVFGILTSSSNNTNQDALAALKTLTTAQAATYNQNYPSAGLGAPGSCQTGAPTETVGGNTHLLYSWAGTAIQPTISVFGVTGATDTSTIPLVDPANALDPSTLALFGTGTVMVNRGSGQNDGVVSKCSALYGQVLSTSYKWNHLDEINQLLGVRGANAEDPVAVIRTHANRLKLAGV
UniProt
P22088
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation

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