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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4OR5

Crystal structure of HIV-1 Tat complexed with human P-TEFb and AFF4

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	0001070	molecular_function	RNA-binding transcription regulator activity
C	0042025	cellular_component	host cell nucleus
C	0050434	biological_process	positive regulation of viral transcription
E	0010468	biological_process	regulation of gene expression
F	0004672	molecular_function	protein kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0006357	biological_process	regulation of transcription by RNA polymerase II
G	0016538	molecular_function	cyclin-dependent protein serine/threonine kinase regulator activity
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
J	0010468	biological_process	regulation of gene expression

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE YT3 A 401

Chain	Residue
A	ASP149
A	ASP167
A	HOH521
A	HOH527

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE YT3 A 402

Chain	Residue
A	ASP305
A	ASP308
A	HOH514

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE YT3 A 403

Chain	Residue
A	HOH505
B	ASP169
B	YT3302
E	YT3101
A	GLU266
A	LYS269

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 404

Chain	Residue
A	LYS48
A	GLU66
A	PHE103
A	ALA166
A	ASP167

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE YT3 B 301

Chain	Residue
B	ASP169
B	GLN172
B	HOH410
E	ARG69
E	YT3101

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE YT3 B 302

Chain	Residue
A	GLU266
A	YT3403
B	ASP169
E	ASP64
E	YT3101

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE YT3 B 303

Chain	Residue
B	GLU17
B	GLU20
B	GLU240
B	GLN243

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 304

Chain	Residue
B	SER167
B	LEU170
B	TRP210
E	TYR59
E	LYS63

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 101

Chain	Residue
C	CYS22
C	HIS33
C	CYS34
C	CYS37

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 102

Chain	Residue
B	CYS261
C	CYS25
C	CYS27
C	CYS30

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE YT3 E 101

Chain	Residue
A	GLU263
A	GLU266
A	YT3403
A	HOH502
B	YT3301
B	YT3302
E	ARG69

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE YT3 E 102

Chain	Residue
A	GLU251
E	GLU37

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE YT3 F 401

Chain	Residue
A	ASN311
A	HOH501
F	ASP305
F	ASP307
F	ASP308

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE YT3 F 402

Chain	Residue
F	ASP149
F	ASP167
F	HOH501
F	HOH502

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE YT3 F 403

Chain	Residue
B	GLU124
F	GLU15

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE YT3 F 404

Chain	Residue
F	GLU263
F	GLU266

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F 405

Chain	Residue
F	LYS48
F	PHE103
F	ALA166
F	ASP167

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE YT3 G 301

Chain	Residue
G	GLU17
G	GLU20
G	GLU240
G	GLN243
G	HOH412

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE YT3 G 302

Chain	Residue
G	ASP169
G	GLN172
J	ARG69
J	YT3101
J	HOH201

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE YT3 G 303

Chain	Residue
G	ASP169
J	ASP64
J	YT3101
J	HOH202

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 G 304

Chain	Residue
G	SER167
G	ASP169
G	LEU170
G	TRP210
J	TYR59
J	LYS63

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN H 101

Chain	Residue
H	CYS22
H	HIS33
H	CYS34
H	CYS37

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN H 102

Chain	Residue
G	CYS261
H	CYS25
H	CYS27
H	CYS30

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE YT3 J 101

Chain	Residue
G	YT3302
G	YT3303
J	ARG69

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	14
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_04079, ECO:0000269\|PubMed:20535204, ECO:0000269\|PubMed:24727379

Chain	Residue	Details
C	CYS22
H	CYS27
H	CYS30
H	HIS33
H	CYS34
H	CYS37
C	CYS25
C	CYS27
C	CYS30
C	HIS33
C	CYS34
C	CYS37
H	CYS22
H	CYS25

site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Essential for Tat translocation through the endosomal membrane => ECO:0000255\|HAMAP-Rule:MF_04079

Chain	Residue	Details
C	TRP11
H	TRP11

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; by host PCAF => ECO:0000255\|HAMAP-Rule:MF_04079

Chain	Residue	Details
C	LYS28
H	LYS28
A	ASP167
F	LYS48
F	ASP104
F	ASP167

site_id	SWS_FT_FI4
Number of Residues	2
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
F	LYS44

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A => ECO:0000269\|PubMed:18250157, ECO:0000269\|PubMed:28426094

Chain	Residue	Details
A	LYS48
F	LYS48

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:21533037

Chain	Residue	Details
A	SER175
F	SER175

site_id	SWS_FT_FI7
Number of Residues	2
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
F	TPO186

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PDB entries from 2024-07-24

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