Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6TSE

Crystal Structure of 1-methylindoline-2,3-dione covalently bound to the PH domain of Bruton's tyrosine kinase mutant R28C

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 MG A 201
ChainResidue
AHOH305
AHOH345
AHOH365
BGLU96

site_idAC2
Number of Residues8
Detailsbinding site for residue 72V A 202
ChainResidue
AILE56
ATYR106
ALEU111
ALYS12
APHE30
ALEU37
ATYR39
ASER55

site_idAC3
Number of Residues7
Detailsbinding site for residue 72V A 203
ChainResidue
AASN24
ALYS26
ALYS53
A72V204
BASN130
BARG133
BTYR134

site_idAC4
Number of Residues5
Detailsbinding site for residue 72V A 204
ChainResidue
ALYS12
ASER14
ALYS26
ATYR39
A72V203

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 205
ChainResidue
AHIS143
ACYS154
ACYS155
ACYS165

site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 201
ChainResidue
AGLU96
AHOH366
AHOH414
BHOH305
BHOH320
BHOH323

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 203
ChainResidue
BHIS143
BCYS154
BCYS155
BCYS165

site_idAC8
Number of Residues4
Detailsbinding site for Di-peptide 72V B 202 and ALA B 2
ChainResidue
BALA3
BVAL4
BVAL34
BHIS35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10196129
ChainResidueDetails
BLYS26
BCYS28
BTYR39
BLYS53
ALYS26
ACYS28
ATYR39
ALYS53

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
BCYS155
BCYS165
ACYS165
BHIS143
BCYS154
AHIS143
ACYS154
ACYS155

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

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

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
BSER55
ASER55

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon