Structure of PDB 2ewb Chain A

Receptor sequence
>2ewbA (length=486) Species: 9913 (Bos taurus) [Search protein sequence]
TKGLVLGIYSKEKEEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGK
TRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQI
QDLEIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSED
QEAWQRGVLFASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDV
FIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGK
GITFDSGGISIKAAANMDLMRADMGGAATICSAIVSAAKLDLPINIVGLA
PLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFN
PKVIINAATLTGAMDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRM
PLFEHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDI
AGVMTNKDEVPYLRKGMAGRPTRTLIEFLFRFSQDS
3D structure
PDB2ewb Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K262 R336
Catalytic site (residue number reindexed from 1) K262 R336
Enzyme Commision number 3.4.11.1: leucyl aminopeptidase.
3.4.11.5: prolyl aminopeptidase.
3.4.13.23: cysteinylglycine-S-conjugate dipeptidase.
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 ZN A D255 D332 E334 D255 D332 E334
BS02 ZN A K250 D273 E334 K250 D273 E334
BS03 CO3 A A333 G335 R336 L360 A333 G335 R336 L360
BS04 ZED A K250 D255 K262 N330 D332 E334 L360 T361 I421 K250 D255 K262 N330 D332 E334 L360 T361 I421 MOAD: Ki=0.8uM
PDBbind-CN: -logKd/Ki=6.10,Ki=0.8uM
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004180 carboxypeptidase activity
GO:0008233 peptidase activity
GO:0016805 dipeptidase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
GO:0097718 disordered domain specific binding
Biological Process
GO:0006508 proteolysis
GO:0019538 protein metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ewb, PDBe:2ewb, PDBj:2ewb
PDBsum2ewb
PubMed16519517
UniProtP00727|AMPL_BOVIN Cytosol aminopeptidase (Gene Name=LAP3)

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