Structure of PDB 4dyo Chain A

Receptor sequence

>4dyoA (length=457) Species: 9606 (Homo sapiens)

GKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKW
NIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRS
RRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVH
VERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTERH
HSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNL
HSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLT
ELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPL
FHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTT
IGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFP
SLAENLY

3D structure

• PDB: 4dyo Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Enzyme Commision number: 3.4.11.21: aspartyl 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	ZN	A	D264 E302 H440	D248 E286 H424
BS02	ZN	A	H94 D264 D346	H88 D248 D330
BS03	SD4	A	H94 D264 E301 E302 D346 K374 Y381 H440	H88 D248 E285 E286 D330 K358 Y365 H424

Gene Ontology

Molecular Function

• GO:0004177 aminopeptidase activity
• GO:0005515 protein binding
• GO:0008237 metallopeptidase activity
• GO:0008270 zinc ion binding
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006508 proteolysis
• GO:0006518 peptide metabolic process

Cellular Component

• GO:0005634 nucleus
• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0072562 blood microparticle

External links

• PDB: RCSB:4dyo, PDBe:4dyo, PDBj:4dyo
• PDBsum: 4dyo
• PubMed: 22720794
• UniProt: Q9ULA0|DNPEP_HUMAN Aspartyl aminopeptidase (Gene Name=DNPEP)