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3TPT

Structure of HipA(D309Q) bound to ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000976molecular_functiontranscription cis-regulatory region binding
A0001217molecular_functionDNA-binding transcription repressor activity
A0003677molecular_functionDNA binding
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006355biological_processregulation of DNA-templated transcription
A0022611biological_processdormancy process
A0032993cellular_componentprotein-DNA complex
A0040008biological_processregulation of growth
A0043565molecular_functionsequence-specific DNA binding
A0044010biological_processsingle-species biofilm formation
A0045892biological_processnegative regulation of DNA-templated transcription
A0046677biological_processresponse to antibiotic
A0106310molecular_functionprotein serine kinase activity
A0110001cellular_componenttoxin-antitoxin complex
B0000287molecular_functionmagnesium ion binding
B0000976molecular_functiontranscription cis-regulatory region binding
B0001217molecular_functionDNA-binding transcription repressor activity
B0003677molecular_functionDNA binding
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006355biological_processregulation of DNA-templated transcription
B0022611biological_processdormancy process
B0032993cellular_componentprotein-DNA complex
B0040008biological_processregulation of growth
B0043565molecular_functionsequence-specific DNA binding
B0044010biological_processsingle-species biofilm formation
B0045892biological_processnegative regulation of DNA-templated transcription
B0046677biological_processresponse to antibiotic
B0106310molecular_functionprotein serine kinase activity
B0110001cellular_componenttoxin-antitoxin complex
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ADP A 500
ChainResidue
AVAL98
AVAL233
AGLU234
AARG235
APHE236
AASP237
ALYS313
AASN314
ATYR331
AASP332
AMG441
AVAL151
AHOH442
AHOH465
AHOH514
AALA152
AGLY153
AALA154
AGLN155
ALYS157
ALYS181
APRO218

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 441
ChainResidue
AASN314
AASP332
AADP500

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 833
ChainResidue
ASER359
ALYS363
AARG372
AHIS373
AHOH529

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP B 501
ChainResidue
BVAL98
BVAL151
BALA152
BGLY153
BALA154
BGLN155
BLYS157
BILE179
BLYS181
BPRO218
BVAL233
BGLU234
BARG235
BPHE236
BASP237
BGLN252
BLYS313
BASN314
BTYR331
BASP332
BMG441
BMG442
BHOH444
BHOH471
BHOH514
BHOH536

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 441
ChainResidue
BGLN155
BASP332
BADP501

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 442
ChainResidue
BASN314
BASP332
BHOH444
BADP501
BHOH536

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 834
ChainResidue
BALA358
BSER359
BLYS363
BARG372
BHIS373

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsDNA_BIND: DNA_BIND => ECO:0000269|PubMed:19150849
ChainResidueDetails
BLYS379-ARG382
ALYS379-ARG382

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17041039
ChainResidueDetails
AGLN309
BGLN309

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22999936, ECO:0007744|PDB:3DNT, ECO:0007744|PDB:3FBR, ECO:0007744|PDB:3HZI, ECO:0007744|PDB:3TPT
ChainResidueDetails
AHIS311
ATYR331
BALA152
BGLU234
BHIS311
BTYR331
AALA152
AGLU234

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22999936, ECO:0007744|PDB:3DNT, ECO:0007744|PDB:3HZI, ECO:0007744|PDB:3TPT
ChainResidueDetails
ALYS181
BLYS181

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:17041039, ECO:0000269|PubMed:22999936
ChainResidueDetails
ASER150
BSER150

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PDB entries from 2024-05-15

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