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6B3W

Structure of Hs/AcPRC2 in complex with 5,8-dichloro-7-(3,5-dimethyl-1,2-oxazol-4-yl)-2-[(4,6-dimethyl-2-oxo-1,2-dihydropyridin-3-yl)methyl]-3,4-dihydroisoquinolin-1(2H)-one

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 Residues6
Detailsbinding site for residue ZN A 701
ChainResidue
ACYS420
AHIS422
ACYS427
ACYS431
AZN702
AZN703

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 702
ChainResidue
ACYS444
AZN701
ACYS420
ACYS433
ACYS440

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 703
ChainResidue
ACYS427
ACYS440
ACYS446
ACYS450
AZN701

site_idAC4
Number of Residues6
Detailsbinding site for residue ZN A 704
ChainResidue
ACYS457
ACYS459
ACYS463
ACYS468
AZN705
AZN706

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN A 705
ChainResidue
ACYS463
ACYS477
ACYS485
ACYS498
AZN704

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN A 706
ChainResidue
ACYS457
ACYS470
ACYS477
ACYS482
AZN704

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN A 707
ChainResidue
ACYS274
ACYS277
ACYS282
AHIS285

site_idAC8
Number of Residues12
Detailsbinding site for residue CJG A 708
ChainResidue
AILE109
ATYR111
AGLY520
ATRP521
ATYR555
ATYR558
APHE562
ATHR575
AARG582
APHE583
AALA584
AASN585

site_idAC9
Number of Residues6
Detailsbinding site for residue ZN B 701
ChainResidue
BCYS427
BCYS440
BCYS446
BCYS450
BZN702
BZN703

site_idAD1
Number of Residues6
Detailsbinding site for residue ZN B 702
ChainResidue
BCYS420
BCYS433
BCYS440
BCYS444
BZN701
BZN703

site_idAD2
Number of Residues6
Detailsbinding site for residue ZN B 703
ChainResidue
BCYS420
BHIS422
BCYS427
BCYS431
BZN701
BZN702

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN B 704
ChainResidue
BCYS457
BCYS470
BCYS477
BCYS482

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN B 705
ChainResidue
BCYS463
BCYS477
BCYS485
BCYS498

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN B 706
ChainResidue
BCYS457
BCYS459
BCYS463
BCYS468

site_idAD6
Number of Residues4
Detailsbinding site for residue ZN B 707
ChainResidue
BCYS274
BCYS277
BCYS282
BHIS285

site_idAD7
Number of Residues11
Detailsbinding site for residue CJG B 708
ChainResidue
BILE109
BTYR111
BGLY520
BTRP521
BTYR555
BTYR558
BPHE562
BARG582
BPHE583
BALA584
BASN585

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

222415

PDB entries from 2024-07-10

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