eF-site ID 2z0p-ABCD PDB Code 2z0p Chain A, B, C, D click to enlarge Title Crystal structure of PH domain of Bruton's tyrosine kinase Classification SIGNALING PROTEIN Compound Tyrosine-protein kinase BTK Source Homo sapiens (Human) (BTK_HUMAN) Sequence A:  AAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYE YDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIME QISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKN VIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQIL B:  AAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYE YDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIEM EQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLK NVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILE N C:  AAVILESIFLKRSQQKLNFKKRLFLLTVHKLSYYEYDFER GRRGSKKGSIDVEKITCVETVVPEKNPPPERQIMEQISII ERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYN SDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILEN D:  AAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYE YDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPM EQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLK NVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILE N Description Functional site 1) chain A residue 143 type sequence H description BINDING SITE FOR RESIDUE ZN A 301 source : AC1 2) chain A residue 154 type sequence C description BINDING SITE FOR RESIDUE ZN A 301 source : AC1 3) chain A residue 155 type sequence C description BINDING SITE FOR RESIDUE ZN A 301 source : AC1 4) chain A residue 165 type sequence C description BINDING SITE FOR RESIDUE ZN A 301 source : AC1 5) chain B residue 143 type sequence H description BINDING SITE FOR RESIDUE ZN B 302 source : AC2 6) chain B residue 154 type sequence C description BINDING SITE FOR RESIDUE ZN B 302 source : AC2 7) chain B residue 155 type sequence C description BINDING SITE FOR RESIDUE ZN B 302 source : AC2 8) chain B residue 165 type sequence C description BINDING SITE FOR RESIDUE ZN B 302 source : AC2 9) chain C residue 143 type sequence H description BINDING SITE FOR RESIDUE ZN C 303 source : AC3 10) chain C residue 152 type sequence Y description BINDING SITE FOR RESIDUE ZN C 303 source : AC3 11) chain C residue 154 type sequence C description BINDING SITE FOR RESIDUE ZN C 303 source : AC3 12) chain C residue 155 type sequence C description BINDING SITE FOR RESIDUE ZN C 303 source : AC3 13) chain C residue 165 type sequence C description BINDING SITE FOR RESIDUE ZN C 303 source : AC3 14) chain D residue 143 type sequence H description BINDING SITE FOR RESIDUE ZN D 304 source : AC4 15) chain D residue 154 type sequence C description BINDING SITE FOR RESIDUE ZN D 304 source : AC4 16) chain D residue 155 type sequence C description BINDING SITE FOR RESIDUE ZN D 304 source : AC4 17) chain D residue 165 type sequence C description BINDING SITE FOR RESIDUE ZN D 304 source : AC4 18) chain A residue 12 type sequence K description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 19) chain A residue 14 type sequence S description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 20) chain A residue 15 type sequence Q description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 21) chain A residue 16 type sequence Q description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 22) chain A residue 17 type sequence K description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 23) chain A residue 18 type sequence K description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 24) chain A residue 21 type sequence S description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 25) chain A residue 22 type sequence P description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 26) chain A residue 24 type sequence N description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 27) chain A residue 26 type sequence K description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 28) chain A residue 28 type sequence R description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 29) chain A residue 39 type sequence Y description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 30) chain A residue 53 type sequence K description BINDING SITE FOR RESIDUE 4PT A 501 source : AC5 31) chain B residue 12 type sequence K description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 32) chain B residue 14 type sequence S description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 33) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 34) chain B residue 16 type sequence Q description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 35) chain B residue 17 type sequence K description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 36) chain B residue 18 type sequence K description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 37) chain B residue 20 type sequence T description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 38) chain B residue 21 type sequence S description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 39) chain B residue 22 type sequence P description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 40) chain B residue 24 type sequence N description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 41) chain B residue 28 type sequence R description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 42) chain B residue 39 type sequence Y description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 43) chain B residue 53 type sequence K description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 44) chain C residue 12 type sequence K description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 45) chain C residue 14 type sequence S description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 46) chain C residue 15 type sequence Q description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 47) chain C residue 16 type sequence Q description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 48) chain C residue 17 type sequence K description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 49) chain C residue 24 type sequence N description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 50) chain C residue 28 type sequence R description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 51) chain C residue 39 type sequence Y description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 52) chain C residue 53 type sequence K description BINDING SITE FOR RESIDUE 4PT C 503 source : AC7 53) chain D residue 12 type sequence K description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 54) chain D residue 14 type sequence S description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 55) chain D residue 15 type sequence Q description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 56) chain D residue 17 type sequence K description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 57) chain D residue 18 type sequence K description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 58) chain D residue 21 type sequence S description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 59) chain D residue 22 type sequence P description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 60) chain D residue 24 type sequence N description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 61) chain D residue 28 type sequence R description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 62) chain D residue 39 type sequence Y description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 63) chain D residue 53 type sequence K description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 64) chain A residue 26 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 65) chain C residue 28 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 66) chain C residue 39 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 67) chain C residue 53 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 68) chain D residue 26 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 69) chain D residue 28 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 70) chain D residue 39 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 71) chain D residue 53 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 72) chain A residue 28 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 39 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 74) chain A residue 53 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 75) chain B residue 26 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 28 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 77) chain B residue 39 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 78) chain B residue 53 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 79) chain C residue 26 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 80) chain A residue 21 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 81) chain A residue 115 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 82) chain B residue 21 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 83) chain B residue 115 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 84) chain C residue 115 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 85) chain D residue 21 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 86) chain D residue 115 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 87) chain A residue 143 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 88) chain C residue 154 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 89) chain C residue 155 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 90) chain C residue 165 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 91) chain D residue 143 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 92) chain D residue 154 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 93) chain D residue 155 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 94) chain D residue 165 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 95) chain A residue 154 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 96) chain A residue 155 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 97) chain A residue 165 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 98) chain B residue 143 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 99) chain B residue 154 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 100) chain B residue 155 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 101) chain B residue 165 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 102) chain C residue 143 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48 source Swiss-Prot : SWS_FT_FI2 103) chain A residue 2 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.11, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3 104) chain B residue 2 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.11, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3 105) chain C residue 2 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.11, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3 106) chain D residue 2 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.11, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3 107) chain A residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P35991 source Swiss-Prot : SWS_FT_FI5 108) chain B residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P35991 source Swiss-Prot : SWS_FT_FI5 109) chain C residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P35991 source Swiss-Prot : SWS_FT_FI5 110) chain D residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P35991 source Swiss-Prot : SWS_FT_FI5 111) chain A residue 55 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI6 112) chain B residue 55 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI6 113) chain C residue 55 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI6 114) chain D residue 55 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI6

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