eF-site ID 6ggh-AB PDB Code 6ggh Chain A, B click to enlarge Title Human jak1 kinase domain in complex with inhibitor Classification TRANSFERASE Compound Tyrosine-protein kinase JAK1 Source (JAK1_HUMAN) Sequence A:  VDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQ VAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIC TNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQIC KGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI ETDKEXXTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFG VTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTL KEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEG FEALLK B:  TEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTG EQVAVKSLGNHIADLKKEIEILRNLYHENIVKYKGICTGI KLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMD YLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK EXXTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLH ELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGK RLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL LK Description Functional site 1) chain A residue 881 type sequence L description binding site for residue EYQ A 1201 source : AC1 2) chain A residue 882 type sequence G description binding site for residue EYQ A 1201 source : AC1 3) chain A residue 889 type sequence V description binding site for residue EYQ A 1201 source : AC1 4) chain A residue 906 type sequence A description binding site for residue EYQ A 1201 source : AC1 5) chain A residue 957 type sequence E description binding site for residue EYQ A 1201 source : AC1 6) chain A residue 958 type sequence F description binding site for residue EYQ A 1201 source : AC1 7) chain A residue 959 type sequence L description binding site for residue EYQ A 1201 source : AC1 8) chain A residue 960 type sequence P description binding site for residue EYQ A 1201 source : AC1 9) chain A residue 962 type sequence G description binding site for residue EYQ A 1201 source : AC1 10) chain A residue 966 type sequence E description binding site for residue EYQ A 1201 source : AC1 11) chain A residue 1003 type sequence D description binding site for residue EYQ A 1201 source : AC1 12) chain A residue 1007 type sequence R description binding site for residue EYQ A 1201 source : AC1 13) chain A residue 1008 type sequence N description binding site for residue EYQ A 1201 source : AC1 14) chain A residue 1010 type sequence L description binding site for residue EYQ A 1201 source : AC1 15) chain A residue 1020 type sequence G description binding site for residue EYQ A 1201 source : AC1 16) chain A residue 1021 type sequence D description binding site for residue EYQ A 1201 source : AC1 17) chain B residue 881 type sequence L description binding site for residue EYQ B 1201 source : AC2 18) chain B residue 882 type sequence G description binding site for residue EYQ B 1201 source : AC2 19) chain B residue 906 type sequence A description binding site for residue EYQ B 1201 source : AC2 20) chain B residue 957 type sequence E description binding site for residue EYQ B 1201 source : AC2 21) chain B residue 958 type sequence F description binding site for residue EYQ B 1201 source : AC2 22) chain B residue 959 type sequence L description binding site for residue EYQ B 1201 source : AC2 23) chain B residue 960 type sequence P description binding site for residue EYQ B 1201 source : AC2 24) chain B residue 962 type sequence G description binding site for residue EYQ B 1201 source : AC2 25) chain B residue 966 type sequence E description binding site for residue EYQ B 1201 source : AC2 26) chain B residue 1003 type sequence D description binding site for residue EYQ B 1201 source : AC2 27) chain B residue 1007 type sequence R description binding site for residue EYQ B 1201 source : AC2 28) chain B residue 1008 type sequence N description binding site for residue EYQ B 1201 source : AC2 29) chain B residue 1010 type sequence L description binding site for residue EYQ B 1201 source : AC2 30) chain B residue 1020 type sequence G description binding site for residue EYQ B 1201 source : AC2 31) chain B residue 1021 type sequence D description binding site for residue EYQ B 1201 source : AC2 32) chain B residue 1042 type sequence D description binding site for residue EYQ B 1201 source : AC2 33) chain A residue 1034 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11909529 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 1035 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11909529 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 1034 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11909529 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 1035 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11909529 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 1003 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 1003 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 881 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 881 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 908 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:32750333 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 908 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:32750333 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 881-908 type prosite sequence LGEGHFGKVELCRYDPEGDNTGEQVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGHFGKVElCrydpegdntgeq......VAVK source prosite : PS00107 44) chain A residue 999-1011 type prosite sequence YVHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNVLV source prosite : PS00109

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