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5IJ8

Structure of the primary oncogenic mutant Y641N Hs/AcPRC2 in complex with a pyridone inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0006338biological_processchromatin remodeling
A0042054molecular_functionhistone methyltransferase activity
A0046976molecular_functionhistone H3K27 methyltransferase activity
B0006338biological_processchromatin remodeling
B0042054molecular_functionhistone methyltransferase activity
B0046976molecular_functionhistone H3K27 methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 6BN A 9001
ChainResidue
AILE109
APHE686
AALA687
AASN688
FARG222
FASP223
AMET110
ATYR111
AGLY623
ATRP624
ATYR661
ACYS663
APHE665
AARG685

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 9002
ChainResidue
ACYS523
AHIS525
ACYS530
ACYS534

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 9003
ChainResidue
ACYS523
ACYS536
ACYS543
ACYS547

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 9004
ChainResidue
ACYS530
ACYS543
ACYS549
ACYS553

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN A 9005
ChainResidue
AALA564
AGLN565
ACYS566
ACYS588
AZN9006

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN A 9006
ChainResidue
ACYS566
ACYS580
ACYS588
ACYS601
AZN9005

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN A 9007
ChainResidue
ACYS560
ACYS573
ACYS580
ACYS585

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN A 9008
ChainResidue
ACYS286
ACYS289
ACYS294
AHIS297

site_idAC9
Number of Residues14
Detailsbinding site for residue 6BN B 9001
ChainResidue
BILE109
BMET110
BTYR111
BGLY623
BTRP624
BTYR661
BCYS663
BPHE665
BARG685
BPHE686
BALA687
BASN688
EARG222
EASP223

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 9002
ChainResidue
BCYS530
BCYS543
BCYS549
BCYS553

site_idAD2
Number of Residues5
Detailsbinding site for residue ZN B 9003
ChainResidue
BCYS523
BCYS536
BCYS543
BCYS547
BZN9004

site_idAD3
Number of Residues5
Detailsbinding site for residue ZN B 9004
ChainResidue
BCYS523
BHIS525
BCYS530
BCYS534
BZN9003

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN B 9005
ChainResidue
BCYS560
BCYS573
BCYS580
BCYS585

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN B 9006
ChainResidue
BCYS566
BCYS580
BCYS588
BCYS601

site_idAD6
Number of Residues4
Detailsbinding site for residue ZN B 9007
ChainResidue
BCYS560
BCYS562
BCYS566
BCYS571

site_idAD7
Number of Residues4
Detailsbinding site for residue ZN B 9008
ChainResidue
BCYS286
BCYS289
BCYS294
BHIS297

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSVskDhALRLWNI
ChainResidueDetails
ELEU192-ILE206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
SSER546
TSER546
ELYS270
FLYS183
FLYS254
FLYS270

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336
ChainResidueDetails
SASP583
TASP583
BALA677

229183

PDB entries from 2024-12-18

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