Structure of PDB 1k4y Chain A

Receptor sequence
>1k4yA (length=501) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
PPVVDTVHGKVLGKFVSLEGFAQPVAVFLGVPFAKPPLGSLRFAPPQPAE
SWSHVKNTTSYPPMCSQDAVSGHMLSELFTNRKENIPLKFSEDCLYLNIY
TPADLTKRGRLPVMVWIHGGGLMVGGASTYDGLALSAHENVVVVTIQYRL
GIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIANFGGDPGSVTIFGESA
GGQSVSILLLSPLTKNLFHRAISESGVALLSSLFRKNTKSLAEKIAIEAG
CKTTTSAVMVHCLRQKTEEELMEVTLKMKFMALDLVGDPKENTAFLTTVI
DGVLLPKAPAEILAEKKYNMLPYMVGINQQEFKLDQKTATELLWKSYPIV
NVSKELTPVATEKYLGGTDDPVKKKDLFLDMLADLLFGVPSVNVARHHRD
AGAPTYMYEYRHGDEIFSVLGAPFLKEGATEEEIKLSKMVMKYWANFARN
GNPNGEGLPQWPAYDYKEGYLQIGATTQAAQKLKDKEVAFWTELWAKEAA
R
3D structure
PDB1k4y Structural insights into CPT-11 activation by mammalian carboxylesterases.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G142 G143 G173 S221 A222 L318 E353 H467
Catalytic site (residue number reindexed from 1) G120 G121 G151 S199 A200 L296 E331 H412
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 4PN A N389 W550 N351 W495
Gene Ontology
Molecular Function
GO:0052689 carboxylic ester hydrolase activity
GO:0106435 carboxylesterase activity
Biological Process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005811 lipid droplet

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1k4y, PDBe:1k4y, PDBj:1k4y
PDBsum1k4y
PubMed11967565
UniProtP12337|EST1_RABIT Liver carboxylesterase 1

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