4IMY
The AFF4 scaffold binds human P-TEFb adjacent to HIV 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 | 0004672 | molecular_function | protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
D | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
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 | 0010468 | biological_process | regulation of gene expression |
I | 0010468 | biological_process | regulation of gene expression |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AMP A 401 |
Chain | Residue |
A | ALA46 |
A | LEU156 |
A | ALA166 |
A | ASP167 |
A | PHE168 |
A | GLY169 |
A | LYS48 |
A | GLU66 |
A | LEU70 |
A | VAL79 |
A | PHE103 |
A | ASP104 |
A | PHE105 |
A | CYS106 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AMP C 401 |
Chain | Residue |
C | ALA46 |
C | LYS48 |
C | PHE103 |
C | ASP104 |
C | PHE105 |
C | CYS106 |
C | ALA153 |
C | ASN154 |
C | ASP167 |
C | PHE168 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE AMP E 401 |
Chain | Residue |
E | ALA46 |
E | LYS48 |
E | GLU66 |
E | VAL79 |
E | PHE103 |
E | ASP104 |
E | PHE105 |
E | CYS106 |
E | LEU156 |
E | ASP167 |
E | PHE168 |
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 | 3 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18566585","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine; by EP300/CBP, PCAF/KAT2B and GCN5/KAT2A","evidences":[{"source":"PubMed","id":"17452463","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18250157","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A","evidences":[{"source":"PubMed","id":"18250157","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28426094","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21533037","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphothreonine; by CaMK1D","evidences":[{"source":"PubMed","id":"15965233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18483222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18566585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18829461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20535204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20851342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21448926","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21779453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |