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BioLiP

Structure of PDB 4g1p Chain A

Receptor sequence
>4g1pA (length=479) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFIS
EQLSQSGFHDIKMVDLGIQPPPSTPNLSLPPVILSRFGSDPSKKTVLVYG
HYDVQPAQLEDGWDTEPFKLVIDEAKGIMKGRGVTDDTGPLLSWINVVDA
FKASGQEFPVNLVTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISDN
YWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQV
LGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTS
LYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPAKVFGKFSIRTVP
DMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFNAQFTA
AKKATKLVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHS
INEKLDISNFVGGMKTMAAYLQYYSESPE
3D structure
PDB4g1p Structural and Mechanistic Basis of Substrate Recognition by Novel Di-peptidase Dug1p From Saccromyces cerevesiae
ChainA
Resolution2.547 Å
3D
structure
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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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4g1p, PDBe:4g1p, PDBj:4g1p
PDBsum4g1p
PubMed
UniProtP43616|DUG1_YEAST Cys-Gly metallodipeptidase DUG1 (Gene Name=DUG1)

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