Structure of PDB 1lam Chain A

Receptor sequence
>1lamA (length=484) Species: 9913 (Bos taurus) [Search protein sequence]
TKGLVLGIYSKEKEEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGK
TRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQI
QDLEIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSED
QEAWQRGVLFASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDV
FIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGK
GITFDSGGISIKAAANMDLMRADMGGAATICSAIVSAAKLDLPINIVGLA
PLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFN
PKVIINAATLTGAMDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRM
PLFEHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDI
AGVMTNKDEVPYLRKGMAGRPTRTLIEFLFRFSQ
3D structure
PDB1lam Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D255 D273 E334 K250 D255 D273 E334
BS03 CO3 A A333 E334 G335 R336 L360 A333 E334 G335 R336 L360
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1lam, PDBe:1lam, PDBj:1lam
PDBsum1lam
PubMed7578088
UniProtP00727|AMPL_BOVIN Cytosol aminopeptidase (Gene Name=LAP3)

[Back to BioLiP]