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1YTS

A LIGAND-INDUCED CONFORMATIONAL CHANGE IN THE YERSINIA PROTEIN TYROSINE PHOSPHATASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AASP356
ASER403
AARG404
AALA405
AGLY406
AVAL407
AGLY408
AARG409
AHOH522

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AARG278
ASER388
ASER389
AALA390

site_idPL
Number of Residues9
DetailsTHE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES
ChainResidue
AHIS402
ASER403
AARG404
AALA405
AGLY406
AVAL407
AGLY408
AARG409
ATHR410

site_idWPD
Number of Residues11
DetailsTHE FLEXIBLE LOOP CONTAINING THE PUTATIVE GENERAL ACID, ASP 356, THAT FOLDS OVER THE SULFATE ANION IN THE SULFATE-BOUND STRUCTURE.
ChainResidue
AHIS350
AVAL351
AGLY352
AASN353
ATRP354
APRO355
AASP356
AGLN357
ATHR358
AALA359
AVAL360

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphocysteine intermediate
ChainResidueDetails
ASER403

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1ytw
ChainResidueDetails
AASP356
ATHR410
ASER403
AARG409
AGLU290
AHIS402

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
ASER403nucleofuge, nucleophile
AARG409electrostatic stabiliser, hydrogen bond donor
ATHR410electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-10-09

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