eF-site ID 2z0p-D PDB Code 2z0p Chain D click to enlarge Title Crystal structure of PH domain of Bruton's tyrosine kinase Classification SIGNALING PROTEIN Compound Tyrosine-protein kinase BTK Source null (BTK_HUMAN) Sequence D:  AAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYE YDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPM EQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLK NVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILE N Description Functional site 1) chain D residue 143 type sequence H description BINDING SITE FOR RESIDUE ZN D 304 source : AC4 2) chain D residue 154 type sequence C description BINDING SITE FOR RESIDUE ZN D 304 source : AC4 3) chain D residue 155 type sequence C description BINDING SITE FOR RESIDUE ZN D 304 source : AC4 4) chain D residue 165 type sequence C description BINDING SITE FOR RESIDUE ZN D 304 source : AC4 5) chain D residue 12 type sequence K description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 6) chain D residue 14 type sequence S description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 7) chain D residue 15 type sequence Q description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 8) chain D residue 17 type sequence K description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 9) chain D residue 18 type sequence K description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 10) chain D residue 21 type sequence S description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 11) chain D residue 22 type sequence P description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 12) chain D residue 24 type sequence N description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 13) chain D residue 28 type sequence R description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 14) chain D residue 39 type sequence Y description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 15) chain D residue 53 type sequence K description BINDING SITE FOR RESIDUE 4PT D 504 source : AC8 16) chain D residue 26 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 17) chain D residue 28 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 18) chain D residue 39 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 19) chain D residue 53 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 20) 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 21) 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 22) 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 23) 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 24) 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 25) chain D residue 21 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 26) chain D residue 115 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 27) chain D residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P35991 source Swiss-Prot : SWS_FT_FI5 28) 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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