Structure of PDB 7xvj Chain D

Receptor sequence
>7xvjD (length=377) Species: 746128 (Aspergillus fumigatus) [Search protein sequence]
MIAYHTLTKALLFPDIDQYQHWHHVAPMLAKMLVDGKYSIHQQYEYLCLF
AQLVAPVLGPYPSPGRDVYRCTLGGNMTVELSQNFQRSGSTTRIAFEPVR
YQASVGHDRFNRTSVNAFFSQLQLLVKSVNIELHHLLSEHLTLTAKDERN
LNEEYLTNFQVKTQYVVALDLRKTGIVAKEYFFPGIKCAATGQTGSNACF
GAIRAVDKDGHLDSLCQLIEAHFQQSKIDDAFLCCDLVDPAHTRFKVYIA
DPLVTLARAEEHWTLGGRLTDEDAAVGLEIIRGLWSELGIIQGLLPIMLN
YEMKAGQRLPKPKLYMPLTGIPETKIARIMTAFFQRHDMPEQAEVFMENL
QTRYQAWLSFAYTKEKGPYLSIYYFWP
3D structure
PDB7xvj Enzymatic formation of a prenyl beta-carboline by a fungal indole prenyltransferase.
ChainD
Resolution2.4 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 PO4 D R129 K219 Y221 Y288 K364 Y366 R93 K179 Y181 Y248 K313 Y315
BS02 PO4 D K219 R284 K286 K364 Y431 K179 R244 K246 K313 Y369
BS03 HFI D L109 E116 Y221 Y366 W419 L73 E80 Y181 Y315 W357
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:7xvj, PDBe:7xvj, PDBj:7xvj
PDBsum7xvj
PubMed35767141
UniProtD1D8L6|CDNTP_ASPFM Cyclic dipeptide prenyltransferase (Gene Name=cdpNPT)

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