Structure of PDB 1xxp Chain B

Receptor sequence
>1xxpB (length=283) Species: 630 (Yersinia enterocolitica) [Search protein sequence]
VSPYGPEARAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCR
RQTAVRADLNANYIQVGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVL
ASSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLT
IREAGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKRNMYES
KGSSAVADDSKLRPVIHSRAGVGRTAQLIGAMCMNDSRNSQLSVEDMVSQ
MRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS
3D structure
PDB1xxp Two substrate-targeting sites in the Yersinia protein tyrosine phosphatase co-operate to promote bacterial virulence
ChainB
Resolution3.0 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 W354 D356 H402 S403 R409 T410
Catalytic site (residue number reindexed from 1) E105 W169 D171 H217 S218 R224 T225
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 peptide B R278 K342 T343 Y383 K386 S388 S389 R93 K157 T158 Y198 K201 S203 S204
BS02 peptide B F229 D231 Q357 S403 R404 A405 G406 V407 G408 R409 Q446 F44 D46 Q172 S218 R219 A220 G221 V222 G223 R224 Q261
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:1xxp, PDBe:1xxp, PDBj:1xxp
PDBsum1xxp
PubMed15720545
UniProtP15273|YOPH_YEREN Tyrosine-protein phosphatase YopH (Gene Name=yopH)

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