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	SITE: Essential for interacting with HIV-1 Tat

Chain	Residue	Details
B	CYS261
D	CYS261
F	CYS261

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
B	SER117
D	SER117
F	SER117

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18566585

Chain	Residue	Details
A	LYS48
A	ASP104
A	ASP167
C	LYS48
C	ASP104
C	ASP167
E	LYS48
E	ASP104
E	ASP167

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-acetyllysine; by EP300/CBP, PCAF/KAT2B and GCN5/KAT2A => ECO:0000269|PubMed:17452463, ECO:0000269|PubMed:18250157

Chain	Residue	Details
A	LYS44
C	LYS44
E	LYS44

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A => ECO:0000269|PubMed:18250157, ECO:0000269|PubMed:28426094

Chain	Residue	Details
A	LYS48
C	LYS48
E	LYS48

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:21533037

Chain	Residue	Details
A	SER175
C	SER175
E	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
C	TPO186
E	TPO186

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