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1YPT

CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
B0004725molecular_functionprotein tyrosine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAPL
Number of Residues9
DetailsTHE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES
ChainResidue
AHIS402
ACYS403
AARG404
AALA405
AGLY406
AVAL407
AGLY408
AARG409
ATHR410

site_idBPL
Number of Residues9
DetailsTHE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES
ChainResidue
BHIS402
BCYS403
BARG404
BALA405
BGLY406
BVAL407
BGLY408
BARG409
BTHR410

site_idWPD
Number of Residues11
DetailsTHE FLEXIBLE LOOP FROM MOLECULE B CONTAINING THE PUTATIVE GENERAL ACID, ASP 356, THAT FOLDS OVER THE ACTIVE SITE AND SEQUESTERS THE TUNGSTATE ANION IN THE TUNGSTATE-BOUND STRUCTURE.
ChainResidue
BHIS350
BVAL351
BGLY352
BASN353
BTRP354
BPRO355
BASP356
BGLN357
BTHR358
BALA359
BVAL360

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. IHCraGvgRTA
ChainResidueDetails
AILE401-ALA411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphocysteine intermediate
ChainResidueDetails
ACYS403
BCYS403

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 47
ChainResidueDetails
AGLU290steric role
ATRP354steric role
AASP356hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS402electrostatic stabiliser, hydrogen bond donor
ACYS403nucleofuge, nucleophile
AARG409electrostatic stabiliser, hydrogen bond donor
ATHR410electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues7
DetailsM-CSA 47
ChainResidueDetails
BGLU290steric role
BTRP354steric role
BASP356hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS402electrostatic stabiliser, hydrogen bond donor
BCYS403nucleofuge, nucleophile
BARG409electrostatic stabiliser, hydrogen bond donor
BTHR410electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-04-24

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