eF-site ID 1yvj-A PDB Code 1yvj Chain A click to enlarge Title Crystal structure of the Jak3 kinase domain in complex with a staurosporine analogue Classification TRANSFERASE Compound Tyrosine-protein kinase JAK3 Source Homo sapiens (Human) (JAK3_HUMAN) Sequence A:  PTIFEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVA VKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGP GRPELRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQI CKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKL LPLDKDXXVVREPGQSPIFWYAPESLSDNIFSRQSDVWSF GVVLYELFTYCDKSCSPSAEFLRMMGCERDVPALCRLLEL LEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGP QLDMLWSGSR Description Functional site 1) chain A residue 833 type sequence F description BINDING SITE FOR RESIDUE DTV A 2962 source : AC1 2) chain A residue 855 type sequence K description BINDING SITE FOR RESIDUE DTV A 2962 source : AC1 3) chain A residue 967 type sequence D description BINDING SITE FOR RESIDUE DTV A 2962 source : AC1 4) chain A residue 969 type sequence G description BINDING SITE FOR RESIDUE DTV A 2962 source : AC1 5) chain A residue 988 type sequence Q description BINDING SITE FOR RESIDUE DTV A 2962 source : AC1 6) chain A residue 943 type sequence R description BINDING SITE FOR RESIDUE DTV A 2963 source : AC2 7) chain A residue 973 type sequence L description BINDING SITE FOR RESIDUE DTV A 2963 source : AC2 8) chain A residue 828 type sequence L description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 9) chain A residue 829 type sequence G description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 10) chain A residue 836 type sequence V description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 11) chain A residue 853 type sequence A description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 12) chain A residue 859 type sequence H description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 13) chain A residue 902 type sequence M description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 14) chain A residue 903 type sequence E description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 15) chain A residue 904 type sequence Y description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 16) chain A residue 905 type sequence L description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 17) chain A residue 908 type sequence G description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 18) chain A residue 911 type sequence R description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 19) chain A residue 953 type sequence R description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 20) chain A residue 956 type sequence L description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 21) chain A residue 967 type sequence D description BINDING SITE FOR RESIDUE 4ST A 2000 source : AC3 22) chain A residue 828-855 type prosite sequence LGKGNFGSVELCRYDPLGDNTGALVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVElCrydplgdntgal......VAVK source prosite : PS00107 23) chain A residue 945-957 type prosite sequence CVHRDLAARNILV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDLAARNILV source prosite : PS00109 24) chain A residue 949 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 828 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 855 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 904 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18250158 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 939 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18250158 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 980 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 981 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699 source Swiss-Prot : SWS_FT_FI4

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