Structure of PDB 3kvn Chain X

Receptor sequence
>3kvnX (length=628) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
HHHHLEAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQN
GSGEIFGPTAPMLLGNQLGIAPGDLAASTSPVNAQQGIADGNNWAVGGYR
TDQIYDSITAANGSLIERDNTLLRSRDGYLVDRARQGLGADPNALYYITG
GGNDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTP
ATFGGPLQPFASQLSGTFNAELTAQLSQAGANVIPLNIPLLLKEGMANPA
SFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSKLLFNDSVHPTITG
QRLIADYTYSLLSAPWELTLLPEMAHGTLRAYQDELRSQWQADWENWQNV
GQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGVAA
GFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDDL
KRKFALGGGERSEKGDTNGHLWAFSARLGYDIAQQADSPWHLSPFVSADY
ARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSDTQLFAEY
AHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPE
LSLRGGYNWRKGEDDTQQSVSLALSLDF
3D structure
PDB3kvn Crystal structure of a full-length autotransporter.
ChainX
Resolution2.499 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.1.1: carboxylesterase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 C8E X S14 L15 N147 P188 V288 H289 S20 L21 N153 P194 V294 H295
BS02 C8E X F21 S32 F34 F27 S38 F40
Gene Ontology
Molecular Function
GO:0016298 lipase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0052689 carboxylic ester hydrolase activity
GO:0106435 carboxylesterase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0008610 lipid biosynthetic process
GO:0009247 glycolipid biosynthetic process
GO:0044010 single-species biofilm formation
GO:0048870 cell motility
GO:0071973 bacterial-type flagellum-dependent cell motility
GO:0071978 bacterial-type flagellum-dependent swarming motility
Cellular Component
GO:0009279 cell outer membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3kvn, PDBe:3kvn, PDBj:3kvn
PDBsum3kvn
PubMed20060837
UniProtO33407|ESTA_PSEAE Esterase EstA (Gene Name=estA)

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