eF-site ID 4qah-A PDB Code 4qah Chain A click to enlarge Title The second sphere residue T263 is important for function and activity of PTP1B through modulating WPD loop Classification HYDROLASE Compound Tyrosine-protein phosphatase non-receptor type 1 Source Homo sapiens (Human) (PTN1_HUMAN) Sequence A:  MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKN KNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRS YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLEL ENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKD PSSVDIKKVLLEMRKFRMGLIQKADQLRFSYLAVIEGAKF IMGDSSVQDQWKELSHEDL Description Functional site 1) chain A residue 54 type sequence H description BINDING SITE FOR RESIDUE TRS A 301 source : AC1 2) chain A residue 130 type sequence E description BINDING SITE FOR RESIDUE TRS A 301 source : AC1 3) chain A residue 181 type catalytic sequence D description 469 source MCSA : MCSA1 4) chain A residue 215 type catalytic sequence C description 469 source MCSA : MCSA1 5) chain A residue 221 type catalytic sequence R description 469 source MCSA : MCSA1 6) chain A residue 222 type catalytic sequence S description 469 source MCSA : MCSA1 7) chain A residue 262 type catalytic sequence Q description 469 source MCSA : MCSA1 8) chain A residue 213-223 type prosite sequence VHCSAGIGRSG description TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRSG source prosite : PS00383 9) chain A residue 215 type ACT_SITE sequence C description Phosphocysteine intermediate source Swiss-Prot : SWS_FT_FI1 10) 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 11) 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 12) chain A residue 181 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 13) chain A residue 215 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 262 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|PubMed:2546149 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 20 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 17) 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 18) chain A residue 66 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745 source Swiss-Prot : SWS_FT_FI7 19) 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 20) 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 21) 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

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