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1BWN

PH DOMAIN AND BTK MOTIF FROM BRUTON'S TYROSINE KINASE MUTANT E41K IN COMPLEX WITH INS(1,3,4,5)P4

Functional Information from GO Data
ChainGOidnamespacecontents
A0035556biological_processintracellular signal transduction
B0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 171
ChainResidue
AHIS143
ACYS154
ACYS155
ACYS165

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 171
ChainResidue
BHIS143
BCYS154
BCYS155
BCYS165

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 4IP A 1
ChainResidue
ALYS12
ASER14
AGLN15
AGLN16
ALYS17
ALYS18
ALYS18
ASER21
APRO22
AASN24
ALYS26
AARG28
ATYR39
ALYS53
A4IP172
AHOH187
AHOH195
AHOH196
AHOH222
AHOH251
AHOH261
AHOH271
AHOH338

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 4IP A 172
ChainResidue
A4IP1
ALYS26
AARG28
ALYS41
ALYS41
ASER51
ALYS53
ALYS53
AHOH196
AHOH222
AHOH260
BGLU45

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 4IP B 1
ChainResidue
BLYS12
BSER14
BGLN15
BGLN16
BLYS17
BLYS18
BLYS18
BSER21
BPRO22
BASN24
BARG28
BTYR39
BLYS53
BLYS53
B4IP172
B4IP172
BHOH174
BHOH192
BHOH196
BHOH200
BHOH204
BHOH225
BHOH252

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 4IP B 172
ChainResidue
AGLU45
B4IP1
B4IP1
BLYS26
BLYS26
BARG28
BLYS41
BLYS41
BSER51
BLYS53
BLYS53
BHOH179
BHOH254
BHOH268

site_idZN1
Number of Residues5
DetailsZN BINDING SITE IN THE BTK MOTIF, CHAIN A
ChainResidue
AZN171
AHIS143
ACYS154
ACYS155
ACYS165

site_idZN2
Number of Residues5
DetailsZN BINDING SITE IN THE BTK MOTIF, CHAIN B
ChainResidue
BCYS165
BZN171
BHIS143
BCYS154
BCYS155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10196129
ChainResidueDetails
ALYS26
AARG28
ATYR39
ALYS53
BLYS26
BARG28
BTYR39
BLYS53

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48
ChainResidueDetails
AHIS143
ACYS154
ACYS155
ACYS165
BHIS143
BCYS154
BCYS155
BCYS165

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.11, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16644721
ChainResidueDetails
ASER21
ASER115
BSER21
BSER115

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P35991
ChainResidueDetails
ATYR40
BTYR40

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER55
BSER55

217705

PDB entries from 2024-03-27

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