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4OGR

crystal structure of P-TEFb complex with AFF4 and Tat

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0006357biological_processregulation of transcription by RNA polymerase II
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
C0010468biological_processregulation of gene expression
D0001070molecular_functionRNA-binding transcription regulator activity
D0042025cellular_componenthost cell nucleus
D0050434biological_processpositive regulation of viral transcription
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
F0006357biological_processregulation of transcription by RNA polymerase II
F0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
G0010468biological_processregulation of gene expression
H0001070molecular_functionRNA-binding transcription regulator activity
H0042025cellular_componenthost cell nucleus
H0050434biological_processpositive regulation of viral transcription
I0004672molecular_functionprotein kinase activity
I0005524molecular_functionATP binding
I0006468biological_processprotein phosphorylation
K0006357biological_processregulation of transcription by RNA polymerase II
K0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
L0010468biological_processregulation of gene expression
M0001070molecular_functionRNA-binding transcription regulator activity
M0042025cellular_componenthost cell nucleus
M0050434biological_processpositive regulation of viral transcription
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ADN A 401
ChainResidue
AILE25
AGLY28
AALA46
APHE105
ACYS106
AASP109
AALA153

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ADN E 401
ChainResidue
EASP104
ECYS106
EASP109
EALA153
EASN154
ELEU156
EGLY26
EALA46

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ADN I 401
ChainResidue
IILE25
IGLY28
IALA46
IASP104
ICYS106
IASP109
IALA153
IASN154
ILEU156
IASP167

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 101
ChainResidue
DCYS22
DHIS33
DCYS34
DCYS37

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 102
ChainResidue
BCYS261
DCYS25
DCYS27
DCYS30

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 101
ChainResidue
HCYS22
HHIS33
HCYS34
HCYS37

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 102
ChainResidue
FCYS261
HCYS25
HCYS27
HCYS30

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN M 101
ChainResidue
MCYS22
MHIS33
MCYS34
MCYS37

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN M 102
ChainResidue
KCYS261
MCYS25
MCYS27
MCYS30

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 Residues21
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04079
ChainResidueDetails
DCYS22
HCYS27
HCYS30
HHIS33
HCYS34
HCYS37
MCYS22
MCYS25
MCYS27
MCYS30
MHIS33
DCYS25
MCYS34
MCYS37
DCYS27
DCYS30
DHIS33
DCYS34
DCYS37
HCYS22
HCYS25

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Essential for Tat translocation through the endosomal membrane => ECO:0000255|HAMAP-Rule:MF_04079
ChainResidueDetails
DTRP11
HTRP11
MTRP11

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; by host PCAF => ECO:0000255|HAMAP-Rule:MF_04079
ChainResidueDetails
DLYS28
HLYS28
MLYS28
ELYS48
EASP104
EASP167
ILYS48
IASP104
IASP167

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-acetyllysine; by host EP300 and GCN5L2 => ECO:0000255|HAMAP-Rule:MF_04079
ChainResidueDetails
DLYS50
DLYS51
HLYS50
HLYS51
MLYS50
MLYS51

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Asymmetric dimethylarginine; by host PRMT6 => ECO:0000255|HAMAP-Rule:MF_04079
ChainResidueDetails
DARG52
DARG53
HARG52
HARG53
MARG52
MARG53

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21533037
ChainResidueDetails
ASER175
ESER175
ISER175

site_idSWS_FT_FI7
Number of Residues3
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
ETPO186
ITPO186

222926

PDB entries from 2024-07-24

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