6HAX

Crystal structure of PROTAC 2 in complex with the bromodomain of human SMARCA2 and pVHL:ElonginC:ElonginB

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006338	biological_process	chromatin remodeling
A	0016586	cellular_component	RSC-type complex
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
D	0006368	biological_process	transcription elongation by RNA polymerase II
D	0030891	cellular_component	VCB complex
D	0070449	cellular_component	elongin complex
E	0006338	biological_process	chromatin remodeling
E	0016586	cellular_component	RSC-type complex
G	0006511	biological_process	ubiquitin-dependent protein catabolic process
H	0006368	biological_process	transcription elongation by RNA polymerase II
H	0030891	cellular_component	VCB complex
H	0070449	cellular_component	elongin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue EDO A 1501

Chain	Residue
A	GLY1467
A	GLN1469
A	GLU1472

---

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 1502

Chain	Residue
A	VAL1408
A	HOH1601
B	FWZ301

---

site_id	AC3
Number of Residues	26
Details	binding site for residue FWZ B 301

Chain	Residue
A	TYR1421
A	VAL1429
A	ALA1460
A	PHE1463
A	ASN1464
A	ILE1470
A	EDO1502
A	HOH1601
B	ARG69
B	TRP88
B	PHE91
B	TYR98
B	PRO99
B	ARG107
B	ILE109
B	HIS110
B	SER111
B	TYR112
B	HIS115
B	TRP117
B	EDO302
B	EDO304
B	HOH412
A	VAL1408
A	PHE1409
A	LEU1418

---

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO B 302

Chain	Residue
B	PRO97
B	TYR98
B	PRO99
B	FWZ301

---

site_id	AC5
Number of Residues	2
Details	binding site for residue EDO B 303

Chain	Residue
B	ASP126
B	ARG161

---

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO B 304

Chain	Residue
B	ARG108
B	ILE109
B	HIS110
B	FWZ301

---

site_id	AC7
Number of Residues	6
Details	binding site for residue EPE B 305

Chain	Residue
B	ASP179
B	ILE180
B	VAL181
B	ARG182
B	SER183
E	ARG1426

---

site_id	AC8
Number of Residues	3
Details	binding site for residue EDO C 201

Chain	Residue
C	ILE65
C	GLU102
C	ALA106

---

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO D 201

Chain	Residue
A	GLU1466
D	TYR45
D	ASP48
D	LEU88

---

site_id	AD1
Number of Residues	2
Details	binding site for residue EDO D 202

Chain	Residue
D	PHE25
D	GLY54

---

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO E 1501

Chain	Residue
E	VAL1408
F	FWZ301

---

site_id	AD3
Number of Residues	24
Details	binding site for residue FWZ F 301

Chain	Residue
E	VAL1408
E	PHE1409
E	TYR1421
E	VAL1429
E	ALA1460
E	PHE1463
E	ASN1464
E	ILE1470
E	EDO1501
F	ARG69
F	TRP88
F	PHE91
F	TYR98
F	PRO99
F	ARG107
F	ILE109
F	HIS110
F	SER111
F	TYR112
F	HIS115
F	TRP117
F	EDO302
F	HOH407
F	HOH412

---

site_id	AD4
Number of Residues	4
Details	binding site for residue EDO F 302

Chain	Residue
F	GLN96
F	PRO97
F	TYR98
F	FWZ301

---

site_id	AD5
Number of Residues	4
Details	binding site for residue EDO G 201

Chain	Residue
G	LYS72
G	PRO94
H	GLN70
H	ALA71

---

site_id	AD6
Number of Residues	3
Details	binding site for residue EDO H 201

Chain	Residue
H	ASP48
H	LEU88
H	ILE90

---

site_id	AD7
Number of Residues	3
Details	binding site for residue EDO H 202

Chain	Residue
H	ARG8
H	PRO92
H	PHE93

---

site_id	AD8
Number of Residues	4
Details	binding site for residue EDO H 203

Chain	Residue
H	ARG43
H	PHE85
E	GLU1450
E	MET1454

---

Functional Information from PROSITE/UniProt

site_id	PS00633
Number of Residues	58
Details	BROMODOMAIN_1 Bromodomain signature. SevFiqlpSrkelp..EYYelIrkpVdfkkIkerirnhk..Yrslgdlekdvml.LchNAqtF

Chain	Residue	Details
A	SER1406-PHE1463

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"39570797","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9E30","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"39570797","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9E31","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	110
Details	Region: {"description":"Involved in binding to CCT complex"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	18
Details	Region: {"description":"Interaction with Elongin BC complex"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	130
Details	Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---