4OGR
crystal structure of P-TEFb complex with AFF4 and Tat
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
B | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
C | 0010468 | biological_process | regulation of gene expression |
D | 0001070 | molecular_function | RNA-binding transcription regulator activity |
D | 0042025 | cellular_component | host cell nucleus |
D | 0050434 | biological_process | positive regulation of viral transcription |
E | 0004672 | molecular_function | protein kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
F | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
G | 0010468 | biological_process | regulation of gene expression |
H | 0001070 | molecular_function | RNA-binding transcription regulator activity |
H | 0042025 | cellular_component | host cell nucleus |
H | 0050434 | biological_process | positive regulation of viral transcription |
I | 0004672 | molecular_function | protein kinase activity |
I | 0005524 | molecular_function | ATP binding |
I | 0006468 | biological_process | protein phosphorylation |
K | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
K | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
L | 0010468 | biological_process | regulation of gene expression |
M | 0001070 | molecular_function | RNA-binding transcription regulator activity |
M | 0042025 | cellular_component | host cell nucleus |
M | 0050434 | biological_process | positive regulation of viral transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ADN A 401 |
Chain | Residue |
A | ILE25 |
A | GLY28 |
A | ALA46 |
A | PHE105 |
A | CYS106 |
A | ASP109 |
A | ALA153 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ADN E 401 |
Chain | Residue |
E | ASP104 |
E | CYS106 |
E | ASP109 |
E | ALA153 |
E | ASN154 |
E | LEU156 |
E | GLY26 |
E | ALA46 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ADN I 401 |
Chain | Residue |
I | ILE25 |
I | GLY28 |
I | ALA46 |
I | ASP104 |
I | CYS106 |
I | ASP109 |
I | ALA153 |
I | ASN154 |
I | LEU156 |
I | ASP167 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 101 |
Chain | Residue |
D | CYS22 |
D | HIS33 |
D | CYS34 |
D | CYS37 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 102 |
Chain | Residue |
B | CYS261 |
D | CYS25 |
D | CYS27 |
D | CYS30 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN H 101 |
Chain | Residue |
H | CYS22 |
H | HIS33 |
H | CYS34 |
H | CYS37 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN H 102 |
Chain | Residue |
F | CYS261 |
H | CYS25 |
H | CYS27 |
H | CYS30 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN M 101 |
Chain | Residue |
M | CYS22 |
M | HIS33 |
M | CYS34 |
M | CYS37 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN M 102 |
Chain | Residue |
K | CYS261 |
M | CYS25 |
M | CYS27 |
M | CYS30 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGTFGEVFkArhrktgqk..........VALK |
Chain | Residue | Details |
A | ILE25-LYS48 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDMKaaNVLI |
Chain | Residue | Details |
A | ILE145-ILE157 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 21 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04079 |
Chain | Residue | Details |
D | CYS22 | |
H | CYS27 | |
H | CYS30 | |
H | HIS33 | |
H | CYS34 | |
H | CYS37 | |
M | CYS22 | |
M | CYS25 | |
M | CYS27 | |
M | CYS30 | |
M | HIS33 | |
D | CYS25 | |
M | CYS34 | |
M | CYS37 | |
D | CYS27 | |
D | CYS30 | |
D | HIS33 | |
D | CYS34 | |
D | CYS37 | |
H | CYS22 | |
H | CYS25 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | SITE: Essential for Tat translocation through the endosomal membrane => ECO:0000255|HAMAP-Rule:MF_04079 |
Chain | Residue | Details |
D | TRP11 | |
H | TRP11 | |
M | TRP11 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine; by host PCAF => ECO:0000255|HAMAP-Rule:MF_04079 |
Chain | Residue | Details |
D | LYS28 | |
H | LYS28 | |
M | LYS28 | |
E | LYS48 | |
E | ASP104 | |
E | ASP167 | |
I | LYS48 | |
I | ASP104 | |
I | ASP167 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine; by host EP300 and GCN5L2 => ECO:0000255|HAMAP-Rule:MF_04079 |
Chain | Residue | Details |
D | LYS50 | |
D | LYS51 | |
H | LYS50 | |
H | LYS51 | |
M | LYS50 | |
M | LYS51 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: Asymmetric dimethylarginine; by host PRMT6 => ECO:0000255|HAMAP-Rule:MF_04079 |
Chain | Residue | Details |
D | ARG52 | |
D | ARG53 | |
H | ARG52 | |
H | ARG53 | |
M | ARG52 | |
M | ARG53 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:21533037 |
Chain | Residue | Details |
A | SER175 | |
E | SER175 | |
I | SER175 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | MOD_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 |
Chain | Residue | Details |
A | TPO186 | |
E | TPO186 | |
I | TPO186 |