eF-site ID 4gl9-C PDB Code 4gl9 Chain C 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 C:  QFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVK KLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSNLR LIMEYLPYGSLRDYLQKHKERIDHKKLLQYTSQICKGMEY LGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKE XXKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYE LFTYIEKSKSPPVEFMRMIGNDKQGQMIVFHLIELLKSNG RLPRPEGCPDEIYVIMTECWNNNVSQRPSFRDLSLRVDQI RDSI Description (1)  Tyrosine-protein kinase (E.C.2.7.10.2), GP130, SOCS3 Functional site 1) chain C residue 934 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 1202 source : AC3 2) chain C residue 944 type sequence H description BINDING SITE FOR RESIDUE PO4 B 1202 source : AC3 3) chain C residue 947 type sequence R description BINDING SITE FOR RESIDUE PO4 B 1202 source : AC3 4) chain C residue 855 type sequence L description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 5) chain C residue 857 type sequence K description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 6) chain C residue 858 type sequence G description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 7) chain C residue 880 type sequence A description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 8) chain C residue 929 type sequence M description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 9) chain C residue 930 type sequence E description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 10) chain C residue 932 type sequence L description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 11) chain C residue 980 type sequence R description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 12) chain C residue 994 type sequence D description BINDING SITE FOR RESIDUE IZA C 1201 source : AC4 13) chain C 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 C residue 855 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 15) chain C residue 882 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 16) chain C residue 966 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20304997 source Swiss-Prot : SWS_FT_FI3 17) chain C residue 972 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20304997 source Swiss-Prot : SWS_FT_FI3 18) chain C residue 1008 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20304997 source Swiss-Prot : SWS_FT_FI3 19) chain C residue 868 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20304997 source Swiss-Prot : SWS_FT_FI3 20) chain C 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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