Structure of PDB 1xxv Chain A

Receptor sequence
>1xxvA (length=282) Species: 630 (Yersinia enterocolitica) [Search protein sequence]
SPYGPEARAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCRR
QTAVRADLNANYIQVGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLA
SSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTI
REAGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKRNMYESK
GSSAVADDSKLRPVIHCRAGVGRTAQLIGAMCMNDSRNSQLSVEDMVSQM
RVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS
3D structure
PDB1xxv Two substrate-targeting sites in the Yersinia protein tyrosine phosphatase co-operate to promote bacterial virulence
ChainA
Resolution2.5 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 C403 R409 T410
Catalytic site (residue number reindexed from 1) E104 W168 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 peptide A F229 R230 D231 I232 C403 R404 A405 V407 G408 R409 Q446 F43 R44 D45 I46 C217 R218 A219 V221 G222 R223 Q260
BS02 peptide A R278 K342 T343 Y383 K386 S388 S389 R92 K156 T157 Y197 K200 S202 S203
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:1xxv, PDBe:1xxv, PDBj:1xxv
PDBsum1xxv
PubMed15720545
UniProtP15273|YOPH_YEREN Tyrosine-protein phosphatase YopH (Gene Name=yopH)

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