eF-site ID 1ypt-B PDB Code 1ypt Chain B click to enlarge Title CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE Classification HYDROLASE Compound PROTEIN-TYROSINE PHOSPHATASE YERSINIA (CATALYTIC DOMAIN) Source Yersinia enterocolitica (YOPH_YEREN) Sequence B:  YGPEARAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNR FRDIQCRRQTAVRADLNANYIQVGNTRTIACQYPLQSQLE SHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTY GSITVESKMTQQVGLGDGIMADMYTLTIREAGQKTISVPV VHVGNWPDQTAVSSEVTKALASLVDQTAETKRNMYESKGS SAVADDSKLRPVIHCRAGVGRTAQLIGAMCMNDSRNSQLS VEDMVSQMRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS Description Functional site 1) chain B residue 402 type sequence H description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 2) chain B residue 403 type sequence C description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 3) chain B residue 404 type sequence R description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 4) chain B residue 405 type sequence A description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 5) chain B residue 406 type sequence G description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 6) chain B residue 407 type sequence V description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 7) chain B residue 408 type sequence G description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 8) chain B residue 409 type sequence R description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 9) chain B residue 410 type sequence T description THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE PHOSPHATASES source : BPL 10) chain B residue 350 type sequence H description THE 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. source : WPD 11) chain B residue 351 type sequence V description THE 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. source : WPD 12) chain B residue 352 type sequence G description THE 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. source : WPD 13) chain B residue 353 type sequence N description THE 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. source : WPD 14) chain B residue 354 type sequence W description THE 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. source : WPD 15) chain B residue 355 type sequence P description THE 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. source : WPD 16) chain B residue 356 type sequence D description THE 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. source : WPD 17) chain B residue 357 type sequence Q description THE 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. source : WPD 18) chain B residue 358 type sequence T description THE 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. source : WPD 19) chain B residue 359 type sequence A description THE 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. source : WPD 20) chain B residue 360 type sequence V description THE 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. source : WPD 21) chain B residue 290 type catalytic sequence E description 47 source MCSA : MCSA2 22) chain B residue 354 type catalytic sequence W description 47 source MCSA : MCSA2 23) chain B residue 356 type catalytic sequence D description 47 source MCSA : MCSA2 24) chain B residue 402 type catalytic sequence H description 47 source MCSA : MCSA2 25) chain B residue 403 type catalytic sequence C description 47 source MCSA : MCSA2 26) chain B residue 409 type catalytic sequence R description 47 source MCSA : MCSA2 27) chain B residue 410 type catalytic sequence T description 47 source MCSA : MCSA2 28) chain B residue 403 type ACT_SITE sequence C description Phosphocysteine intermediate source Swiss-Prot : SWS_FT_FI1

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