Structure of PDB 4w4u Chain A

Receptor sequence
>4w4uA (length=438) Species: 889517 (Saccharomyces cerevisiae CEN.PK113-7D) [Search protein sequence]
MSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEKFLNTMKCGTCH
EINSGATFMCLQCGFCGCWNHSHFLSHSKQIGHIFGINSNNGLLFCFKCE
DYIGNIDLINDAILAKYWDDVCTKTMVPSMERRDGLSGLINMGSTCFMSS
ILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALRQ
TGFIYLLTCAWKIQDAHEFWQFIINQIHQSYVLDLPNAKEVSRANNKQCE
CIVHTVFEGSLESSIVCPGCQNNSKTTIDPFLDLSLDIKDKKKLYECLDS
FHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLNGS
NRKLDDFIEFPTYLNMKNYCSTVPDIIYELIGIVSHKGTVNEGHYIAFCK
ISGGQWFKFNDSMVSSISQEEVLKEQAYLLFYTIRQVN
3D structure
PDB4w4u Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N141 C146 H427 N443
Catalytic site (residue number reindexed from 1) N141 C146 H394 N410
Enzyme Commision number 3.4.19.12: ubiquitinyl hydrolase 1.
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 C4 H6 C96 C99 C4 H6 C96 C99
BS02 ZN A C46 C49 C68 H73 C46 C49 C68 H73
BS03 ZN A H250 C271 C273 H276 H228 C249 C251 H254
BS04 ZN A C60 C63 H77 H83 C60 C63 H77 H83
BS05 ZN A H170 C174 C182 C185 H170 C174 C182 C185
BS06 ZN A C289 C292 C336 C339 C267 C270 C314 C317
Gene Ontology
Molecular Function
GO:0004843 cysteine-type deubiquitinase activity
GO:0008234 cysteine-type peptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0016579 protein deubiquitination

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Molecular Function
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Biological Process
External links
PDB RCSB:4w4u, PDBe:4w4u, PDBj:4w4u
PDBsum4w4u
PubMed25526805
UniProtN1P0J5

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