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

3MI9

Crystal structure of HIV-1 Tat complexed with human P-TEFb

Functional Information from GO Data
ChainGOidnamespacecontents
A0000976molecular_functiontranscription cis-regulatory region binding
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0001223molecular_functiontranscription coactivator binding
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003711molecular_functiontranscription elongation factor activity
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006282biological_processregulation of DNA repair
A0006366biological_processtranscription by RNA polymerase II
A0006367biological_processtranscription initiation at RNA polymerase II promoter
A0006368biological_processtranscription elongation by RNA polymerase II
A0006468biological_processprotein phosphorylation
A0007346biological_processregulation of mitotic cell cycle
A0008023cellular_componenttranscription elongation factor complex
A0008024cellular_componentcyclin/CDK positive transcription elongation factor complex
A0008283biological_processcell population proliferation
A0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016605cellular_componentPML body
A0017069molecular_functionsnRNA binding
A0019901molecular_functionprotein kinase binding
A0031297biological_processreplication fork processing
A0031440biological_processregulation of mRNA 3'-end processing
A0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
A0036464cellular_componentcytoplasmic ribonucleoprotein granule
A0043923biological_processpositive regulation by host of viral transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0051147biological_processregulation of muscle cell differentiation
A0051647biological_processnucleus localization
A0051726biological_processregulation of cell cycle
A0070691cellular_componentP-TEFb complex
A0071345biological_processcellular response to cytokine stimulus
A0097322molecular_function7SK snRNA binding
A0106310molecular_functionprotein serine kinase activity
A0120186biological_processnegative regulation of protein localization to chromatin
A0120187biological_processpositive regulation of protein localization to chromatin
A0140673biological_processtranscription elongation-coupled chromatin remodeling
B0006357biological_processregulation of transcription by RNA polymerase II
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
C0001070molecular_functionRNA-binding transcription regulator activity
C0003723molecular_functionRNA binding
C0004865molecular_functionprotein serine/threonine phosphatase inhibitor activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0006351biological_processDNA-templated transcription
C0006915biological_processapoptotic process
C0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
C0019049biological_processvirus-mediated perturbation of host defense response
C0019904molecular_functionprotein domain specific binding
C0030332molecular_functioncyclin binding
C0030430cellular_componenthost cell cytoplasm
C0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
C0039502biological_processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
C0039525biological_processmodulation by virus of host chromatin organization
C0039606biological_processsymbiont-mediated suppression of host translation initiation
C0042025cellular_componenthost cell nucleus
C0042783biological_processevasion of host immune response
C0042805molecular_functionactinin binding
C0044196cellular_componenthost cell nucleolus
C0046872molecular_functionmetal ion binding
C0050434biological_processpositive regulation of viral transcription
C0052170biological_processsymbiont-mediated suppression of host innate immune response
C0140313molecular_functionmolecular sequestering activity
C1990970molecular_functiontrans-activation response element binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 87
ChainResidue
CCYS22
CHIS33
CCYS34
CCYS37

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 88
ChainResidue
BCYS261
CCYS25
CCYS27
CCYS30

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGTFGEVFkArhrktgqk..........VALK
ChainResidueDetails
AILE25-LYS48

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDMKaaNVLI
ChainResidueDetails
AILE145-ILE157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:20535204, ECO:0000269|PubMed:24727379
ChainResidueDetails
CCYS22
CCYS25
CCYS27
CCYS30
CHIS33
CCYS34
CCYS37

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Essential for Tat translocation through the endosomal membrane => ECO:0000255|HAMAP-Rule:MF_04079
ChainResidueDetails
CTRP11

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by host PCAF => ECO:0000255|HAMAP-Rule:MF_04079
ChainResidueDetails
CLYS28
AASP104
AASP167

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; by host EP300 and GCN5L2 => ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:18480452
ChainResidueDetails
CLYS50
CLYS51

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Asymmetric dimethylarginine; by host PRMT6 => ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:17267505
ChainResidueDetails
CARG52
CARG53

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000255|HAMAP-Rule:MF_04079
ChainResidueDetails
CLYS71

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK1D => ECO:0000269|PubMed:15965233, ECO:0000269|PubMed:18483222, ECO:0000269|PubMed:18566585, ECO:0000269|PubMed:18829461, ECO:0000269|PubMed:20535204, ECO:0000269|PubMed:20851342, ECO:0000269|PubMed:21448926, ECO:0000269|PubMed:21779453, ECO:0007744|PubMed:21406692
ChainResidueDetails
ATPO186

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon