eF-site ID 2z0p-B PDB Code 2z0p Chain B 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 B:  AAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYE YDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIEM EQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLK NVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILE N Description Functional site 1) chain B residue 143 type sequence H description BINDING SITE FOR RESIDUE ZN B 302 source : AC2 2) chain B residue 154 type sequence C description BINDING SITE FOR RESIDUE ZN B 302 source : AC2 3) chain B residue 155 type sequence C description BINDING SITE FOR RESIDUE ZN B 302 source : AC2 4) chain B residue 165 type sequence C description BINDING SITE FOR RESIDUE ZN B 302 source : AC2 5) chain B residue 12 type sequence K description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 6) chain B residue 14 type sequence S description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 7) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 8) chain B residue 16 type sequence Q description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 9) chain B residue 17 type sequence K description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 10) chain B residue 18 type sequence K description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 11) chain B residue 20 type sequence T description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 12) chain B residue 21 type sequence S description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 13) chain B residue 22 type sequence P description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 14) chain B residue 24 type sequence N description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 15) chain B residue 28 type sequence R description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 16) chain B residue 39 type sequence Y description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 17) chain B residue 53 type sequence K description BINDING SITE FOR RESIDUE 4PT B 502 source : AC6 18) chain B residue 26 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 28 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 39 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 53 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10196129 source Swiss-Prot : SWS_FT_FI1 22) 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 23) 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 24) 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 25) 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 26) 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 27) chain B residue 21 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 115 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16644721 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P35991 source Swiss-Prot : SWS_FT_FI5 30) chain B residue 55 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI6

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