eF-site ID 4gl9-B PDB Code 4gl9 Chain B click to enlarge Title Crystal structure of inhibitory protein SOCS3 in complex with JAK2 kinase domain and fragment of GP130 intracellular domain Classification transferase/transferase inhibitor Compound Tyrosine-protein kinase Source (4GL9) Sequence B:  QFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVK KLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSNLR LIMEYLPYGSLRDYLQKHKERIDHKKLLQYTSQICKGMEY LGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKE XXKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYE LFTYKSKSPPVEFMRMIGNDKQGQMIVFHLIELLKSNGRL PRPEGCPDEIYVIMTECWNNNVSQRPSFRDLSLRVDQIRD SI Description (1)  Tyrosine-protein kinase (E.C.2.7.10.2), GP130, SOCS3 Functional site 1) chain B residue 855 type sequence L description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 2) chain B residue 863 type sequence V description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 3) chain B residue 880 type sequence A description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 4) chain B residue 929 type sequence M description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 5) chain B residue 930 type sequence E description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 6) chain B residue 931 type sequence Y description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 7) chain B residue 932 type sequence L description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 8) chain B residue 935 type sequence G description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 9) chain B residue 983 type sequence L description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 10) chain B residue 994 type sequence D description BINDING SITE FOR RESIDUE IZA B 1201 source : AC2 11) chain B residue 985 type sequence E description BINDING SITE FOR RESIDUE PO4 B 1202 source : AC3 12) chain B residue 989 type sequence R description BINDING SITE FOR RESIDUE PO4 B 1202 source : AC3 13) chain B residue 976 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 855 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 882 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 868 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20304997 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 966 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20304997 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 972 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20304997 source Swiss-Prot : SWS_FT_FI3 19) chain B residue 1008 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20304997 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 1007 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:9473212 source Swiss-Prot : SWS_FT_FI4

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