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6W7G

Structure of EED bound to inhibitor 1056

Functional Information from GO Data
ChainGOidnamespacecontents
A0016571biological_processhistone methylation
A0035098cellular_componentESC/E(Z) complex
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue Q3A A 501
ChainResidue
APHE97
AARG414
AHOH751
ATYR148
AASN194
ALYS211
ALEU240
AASP310
ATYR365
AMET366
AARG367

site_idAC2
Number of Residues16
Detailsbinding site for residue Q3A A 502
ChainResidue
AHIS199
AARG201
AASP202
ALEU205
ALEU247
AGLY248
AILE265
AMET271
AILE274
ALYS275
ATYR278
AQ3A503
AHOH740
AHOH744
AHOH773
AHOH786

site_idAC3
Number of Residues10
Detailsbinding site for residue Q3A A 503
ChainResidue
AARG201
AASP212
AALA214
AILE228
AGLY230
AGLY231
AVAL232
ALYS293
AQ3A502
AHOH754

site_idAC4
Number of Residues4
Detailsbinding site for residue NA A 504
ChainResidue
ACYS182
AHIS185
AHOH906
AHOH921

site_idAC5
Number of Residues4
Detailsbinding site for residue FMT A 505
ChainResidue
ALYS184
AILE220
AHOH624
AHOH657

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSVskDhALRLWNI
ChainResidueDetails
ALEU206-ILE220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:20974918
ChainResidueDetails
ALYS197
ALYS268
ALYS284

223532

PDB entries from 2024-08-07

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