Structure of PDB 4g1p Chain A

Receptor sequence

>4g1pA (length=479) Species: 559292 (Saccharomyces cerevisiae S288C)

MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFIS
EQLSQSGFHDIKMVDLGIQPPPSTPNLSLPPVILSRFGSDPSKKTVLVYG
HYDVQPAQLEDGWDTEPFKLVIDEAKGIMKGRGVTDDTGPLLSWINVVDA
FKASGQEFPVNLVTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISDN
YWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQV
LGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTS
LYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPAKVFGKFSIRTVP
DMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFNAQFTA
AKKATKLVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHS
INEKLDISNFVGGMKTMAAYLQYYSESPE

3D structure

• PDB: 4g1p Structural and Mechanistic Basis of Substrate Recognition by Novel Di-peptidase Dug1p From Saccromyces cerevesiae
• Chain: A
• Resolution: 2.547 Å

Enzymatic activity

• Enzyme Commision number: 3.4.13.-

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	D137 E172 H450	D136 E171 H449
BS02	ZN	A	D137 D200	D136 D199
BS03	GLY	A	E171 H450	E170 H449
BS04	CYS	A	C218 R348 H385	C217 R347 H384

Gene Ontology

Molecular Function

• GO:0008233 peptidase activity
• GO:0008237 metallopeptidase activity
• GO:0008242 omega peptidase activity
• GO:0008270 zinc ion binding
• GO:0016787 hydrolase activity
• GO:0016805 dipeptidase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding
• GO:0070573 metallodipeptidase activity

Biological Process

• GO:0006508 proteolysis
• GO:0006751 glutathione catabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005739 mitochondrion

External links

• PDB: RCSB:4g1p, PDBe:4g1p, PDBj:4g1p
• PDBsum: 4g1p
• UniProt: P43616|DUG1_YEAST Cys-Gly metallodipeptidase DUG1 (Gene Name=DUG1)