eF-site ID 5qdp-A PDB Code 5qdp Chain A click to enlarge Title PanDDA analysis group deposition -- Crystal structure of PTP1B in complex with compound_FMOPL000207a Classification HYDROLASE Compound Tyrosine-protein phosphatase non-receptor type 1 Source (PTN1_HUMAN) Sequence A:  MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPSRVAKLPKN KNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRS YILTQGPLPNTVGHFWEMVWEQKSRGVVMLNRVMEKGSLK CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLEL ENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKD PSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKF IM Description Functional site 1) chain A residue 45 type sequence R description binding site for residue JGA A 401 source : AC1 2) chain A residue 118 type sequence S description binding site for residue JGA A 401 source : AC1 3) chain A residue 196 type sequence F description binding site for residue JGA A 401 source : AC1 4) chain A residue 236 type sequence D description binding site for residue JGA A 401 source : AC1 5) chain A residue 281 type sequence I description binding site for residue JGA A 401 source : AC1 6) chain A residue 282 type sequence M description binding site for residue JGA A 401 source : AC1 7) chain A residue 54 type sequence H description binding site for residue TRS A 402 source : AC2 8) chain A residue 128 type sequence K description binding site for residue TRS A 402 source : AC2 9) chain A residue 129 type sequence E description binding site for residue TRS A 402 source : AC2 10) chain A residue 130 type sequence E description binding site for residue TRS A 402 source : AC2 11) chain A residue 181 type catalytic sequence D description 469 source MCSA : MCSA1 12) chain A residue 215 type catalytic sequence C description 469 source MCSA : MCSA1 13) chain A residue 221 type catalytic sequence R description 469 source MCSA : MCSA1 14) chain A residue 222 type catalytic sequence S description 469 source MCSA : MCSA1 15) chain A residue 262 type catalytic sequence Q description 469 source MCSA : MCSA1 16) chain A residue 213-223 type prosite sequence VHCSAGIGRSG description TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRSG source prosite : PS00383 17) chain A residue 215 type ACT_SITE sequence C description Phosphocysteine intermediate source Swiss-Prot : SWS_FT_FI1 18) 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 19) 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 20) chain A residue 181 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 21) chain A residue 215 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 262 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|PubMed:2546149 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 20 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 25) 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 26) chain A residue 66 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745 source Swiss-Prot : SWS_FT_FI7 27) 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 28) 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 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

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