eF-site ID 1c84-A PDB Code 1c84 Chain A click to enlarge Title CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 3-(OXALYL-AMINO)-NAPHTHALENE-2-CARBOXLIC ACID Classification HYDROLASE Compound PROTEIN (PROTEIN-TYROSINE PHOSPHATASE 1B) Source null (PTN1_HUMAN) Sequence A:  EMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNK NRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSY ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKC AQYWPQKEEKEMIFEDTNLKLTLISEDIKTYYTVRQLELE NLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRES GSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDP SSVDIKKVLLDMRKFRMGLIQTADQLRFSYLAVIEGAKFI MGDSSVQDQWKELSHED Description Functional site 1) chain A residue 46 type sequence Y description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 2) chain A residue 49 type sequence V description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 3) chain A residue 120 type sequence K description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 4) chain A residue 181 type sequence D description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 5) chain A residue 182 type sequence F description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 6) chain A residue 215 type sequence C description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 7) chain A residue 216 type sequence S description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 8) chain A residue 217 type sequence A description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 9) chain A residue 219 type sequence I description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 10) chain A residue 220 type sequence G description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 11) chain A residue 221 type sequence R description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 12) chain A residue 262 type sequence Q description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 13) chain A residue 285 type sequence S description BINDING SITE FOR RESIDUE 761 A 301 source : AC1 14) chain A residue 181 type catalytic sequence D description 469 source MCSA : MCSA1 15) chain A residue 215 type catalytic sequence C description 469 source MCSA : MCSA1 16) chain A residue 221 type catalytic sequence R description 469 source MCSA : MCSA1 17) chain A residue 222 type catalytic sequence S description 469 source MCSA : MCSA1 18) chain A residue 262 type catalytic sequence Q description 469 source MCSA : MCSA1 19) chain A residue 213-223 type prosite sequence VHCSAGIGRSG description TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRSG source prosite : PS00383 20) chain A residue 215 type CROSSLNK sequence C description N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339 source Swiss-Prot : SWS_FT_FI10 21) chain A residue 216 type CROSSLNK sequence S description N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339 source Swiss-Prot : SWS_FT_FI10 22) chain A residue 181 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 23) chain A residue 215 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 262 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 20 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 50 type MOD_RES sequence S description Phosphoserine; by PKB/AKT1, CLK1 and CLK2 => ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:11579209, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 66 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 215 type MOD_RES sequence C description S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477 source Swiss-Prot : SWS_FT_FI8 29) chain A residue 243 type MOD_RES sequence S description Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872 source Swiss-Prot : SWS_FT_FI9 30) chain A residue 242 type MOD_RES sequence S description Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872 source Swiss-Prot : SWS_FT_FI9 31) chain A residue 215 type ACT_SITE sequence C description Phosphocysteine intermediate source Swiss-Prot : SWS_FT_FI1

Display surface Download Links