Structure of PDB 4e0u Chain A

Receptor sequence
>4e0uA (length=408) Species: 746128 (Aspergillus fumigatus) [Search protein sequence]
PIPKDIAYHTLTKALLFPDIDQYQHWHHVAPMLAKMLVDGKYSIHQQYEY
LCLFAQLVAPVLGPYPSPGRDVYRCTLGGNMTVELSQNFQRSGSTTRIAF
EPVRYQASVGHDRFNRTSVNAFFSQLQLLVKSVNIELHHLLSEHLTLTAK
DERNLNEEQLTKYLTNFQVKTQYVVALDLRKTGIVAKEYFFPGIKCAATG
QTGSNACFGAIRAVDKDGHLDSLCQLIEAHFQQSKIDDAFLCCDLVDPAH
TRFKVYIADPLVTLARAEEHWTLGGRLTDEDAAVGLEIIRGLWSELGIIQ
GPLEPSAMMEKGLLPIMLNYEMKAGQRLPKPKLYMPLTGIPETKIARIMT
AFFQRHDMPEQAEVFMENLQAYYEGKNLEEATRYQAWLSFAYTKEKGPYL
SIYYFWPE
3D structure
PDB4e0u Structure and catalytic mechanism of a cyclic dipeptide prenyltransferase with broad substrate promiscuity.
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.-
3.4.11.17: tryptophanyl aminopeptidase.
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 0MV A T108 L109 E116 V201 T203 Y221 F223 M349 T76 L77 E84 V169 T171 Y189 F191 M317
BS02 PIS A R129 K219 Y221 R284 K286 Y288 K364 Y366 Y431 Y435 R97 K187 Y189 R252 K254 Y256 K332 Y334 Y399 Y403
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004659 prenyltransferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
Biological Process
GO:0006508 proteolysis
GO:0009820 alkaloid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4e0u, PDBe:4e0u, PDBj:4e0u
PDBsum4e0u
PubMed22683356
UniProtD1D8L6|CDNTP_ASPFM Cyclic dipeptide prenyltransferase (Gene Name=cdpNPT)

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