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6HAX

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0006338biological_processchromatin remodeling
A0016586cellular_componentRSC-type complex
C0006511biological_processubiquitin-dependent protein catabolic process
D0006368biological_processtranscription elongation by RNA polymerase II
D0030891cellular_componentVCB complex
D0070449cellular_componentelongin complex
E0006338biological_processchromatin remodeling
E0016586cellular_componentRSC-type complex
G0006511biological_processubiquitin-dependent protein catabolic process
H0006368biological_processtranscription elongation by RNA polymerase II
H0030891cellular_componentVCB complex
H0070449cellular_componentelongin complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue EDO A 1501
ChainResidue
AGLY1467
AGLN1469
AGLU1472

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 1502
ChainResidue
AVAL1408
AHOH1601
BFWZ301

site_idAC3
Number of Residues26
Detailsbinding site for residue FWZ B 301
ChainResidue
ATYR1421
AVAL1429
AALA1460
APHE1463
AASN1464
AILE1470
AEDO1502
AHOH1601
BARG69
BTRP88
BPHE91
BTYR98
BPRO99
BARG107
BILE109
BHIS110
BSER111
BTYR112
BHIS115
BTRP117
BEDO302
BEDO304
BHOH412
AVAL1408
APHE1409
ALEU1418

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO B 302
ChainResidue
BPRO97
BTYR98
BPRO99
BFWZ301

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO B 303
ChainResidue
BASP126
BARG161

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO B 304
ChainResidue
BARG108
BILE109
BHIS110
BFWZ301

site_idAC7
Number of Residues6
Detailsbinding site for residue EPE B 305
ChainResidue
BASP179
BILE180
BVAL181
BARG182
BSER183
EARG1426

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO C 201
ChainResidue
CILE65
CGLU102
CALA106

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO D 201
ChainResidue
AGLU1466
DTYR45
DASP48
DLEU88

site_idAD1
Number of Residues2
Detailsbinding site for residue EDO D 202
ChainResidue
DPHE25
DGLY54

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO E 1501
ChainResidue
EVAL1408
FFWZ301

site_idAD3
Number of Residues24
Detailsbinding site for residue FWZ F 301
ChainResidue
EVAL1408
EPHE1409
ETYR1421
EVAL1429
EALA1460
EPHE1463
EASN1464
EILE1470
EEDO1501
FARG69
FTRP88
FPHE91
FTYR98
FPRO99
FARG107
FILE109
FHIS110
FSER111
FTYR112
FHIS115
FTRP117
FEDO302
FHOH407
FHOH412

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO F 302
ChainResidue
FGLN96
FPRO97
FTYR98
FFWZ301

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO G 201
ChainResidue
GLYS72
GPRO94
HGLN70
HALA71

site_idAD6
Number of Residues3
Detailsbinding site for residue EDO H 201
ChainResidue
HASP48
HLEU88
HILE90

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO H 202
ChainResidue
HARG8
HPRO92
HPHE93

site_idAD8
Number of Residues4
Detailsbinding site for residue EDO H 203
ChainResidue
HARG43
HPHE85
EGLU1450
EMET1454

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues58
DetailsBROMODOMAIN_1 Bromodomain signature. SevFiqlpSrkelp..EYYelIrkpVdfkkIkerirnhk..Yrslgdlekdvml.LchNAqtF
ChainResidueDetails
ASER1406-PHE1463

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
DMET1
HMET1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62869
ChainResidueDetails
DTHR84
HTHR84

219140

PDB entries from 2024-05-01

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