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5VFC

WDR5 bound to inhibitor MM-589

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000123cellular_componenthistone acetyltransferase complex
A0001501biological_processskeletal system development
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0006094biological_processgluconeogenesis
A0006325biological_processchromatin organization
A0006355biological_processregulation of DNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0035064molecular_functionmethylated histone binding
A0035097cellular_componenthistone methyltransferase complex
A0042393molecular_functionhistone binding
A0042800molecular_functionhistone H3K4 methyltransferase activity
A0044545cellular_componentNSL complex
A0044665cellular_componentMLL1/2 complex
A0044666cellular_componentMLL3/4 complex
A0045722biological_processpositive regulation of gluconeogenesis
A0045815biological_processtranscription initiation-coupled chromatin remodeling
A0045893biological_processpositive regulation of DNA-templated transcription
A0045995biological_processregulation of embryonic development
A0048188cellular_componentSet1C/COMPASS complex
A0051302biological_processregulation of cell division
A0051726biological_processregulation of cell cycle
A0071339cellular_componentMLL1 complex
A0072686cellular_componentmitotic spindle
A0090043biological_processregulation of tubulin deacetylation
A0140672cellular_componentATAC complex
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue 9BA A 401
ChainResidue
ASER49
AGLY254
ALYS259
ATYR260
ACYS261
APHE263
ATHR290
ALYS291
AGLU292
AHOH519
AHOH530
AILE90
AHOH542
AHOH564
AHOH567
AHOH609
ASER91
AASP92
AASP107
APHE133
ACYS134
ASER175
ATHR253

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 402
ChainResidue
AHIS178
ALYS221
AEDO404
AHOH524
AHOH619
AHOH628

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 403
ChainResidue
ALEU143
ALYS165
ATHR200
AALA201

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 404
ChainResidue
ATRP95
ASER97
APHE137
AASN138
ASO4402

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 405
ChainResidue
ATYR228
ALYS250
AGLN289

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 406
ChainResidue
ALYS38
ALYS162
ALYS331
AASP333
AHOH554

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO A 407
ChainResidue
AILE113
ALYS123
AVAL158

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO A 408
ChainResidue
APHE39
AALA74
ATYR75
ALEU329
AHOH656

site_idAC9
Number of Residues1
Detailsbinding site for residue EDO A 409
ChainResidue
AHOH535

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsdDkTLKIWDV
ChainResidueDetails
ALEU102-VAL116
AILE144-VAL158
AILE186-THR200
AILE274-LEU288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Important for interaction with histone H3
ChainResidueDetails
AASP107
APHE133
APHE263
AGLU322

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS112

site_idSWS_FT_FI3
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS27
ALYS46

229183

PDB entries from 2024-12-18

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