Structure of PDB 4zn5 Chain A

Receptor sequence
>4zn5A (length=282) Species: 630 (Yersinia enterocolitica) [Search protein sequence]
SPYGPEARAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCRR
QTAVRADLNANYIQVGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLA
SSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTI
REAGQKTISVPVVHVGNYPDQTAVSSEVTKALASLVDQTAETKRNMYESK
GSSAVADDSKLRPVIHCRAGVGRTAQLIGAMCMNDSRNSQLSVEDMVSQM
RVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS
3D structure
PDB4zn5 Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites.
ChainA
Resolution1.12 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E290 Y354 D356 H402 C403 R409 T410
Catalytic site (residue number reindexed from 1) E104 Y168 D170 H216 C217 R223 T224
Enzyme Commision number 3.1.3.48: protein-tyrosine-phosphatase.
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 DVG A C403 R404 A405 V407 G408 R409 Q446 K447 Q450 C217 R218 A219 V221 G222 R223 Q260 K261 Q264
BS02 VO4 A R278 K342 S388 S389 R92 K156 S202 S203
BS03 GOL A M317 D330 M331 Y332 M131 D144 M145 Y146
Gene Ontology
Molecular Function
GO:0004725 protein tyrosine phosphatase activity
Biological Process
GO:0006470 protein dephosphorylation
GO:0016311 dephosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4zn5, PDBe:4zn5, PDBj:4zn5
PDBsum4zn5
PubMed26445170
UniProtP15273|YOPH_YEREN Tyrosine-protein phosphatase YopH (Gene Name=yopH)

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