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6PDG

Crystal structure of MYST acetyltransferase domain in complex with inhibitor 83

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 801
ChainResidue
ACYS540
ACYS543
AHIS556
ACYS560

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 802
ChainResidue
AASP520
AHOH913
AHOH923
AHOH1039

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 803
ChainResidue
ASER690
ASER693
AO9A806
ALEU689

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 804
ChainResidue
ALYS573
AILE576
AGLN731
AHIS743
AHOH903

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 805
ChainResidue
ATYR517
AARG656
AHOH920
AHOH1007

site_idAC6
Number of Residues17
Detailsbinding site for residue O9A A 806
ChainResidue
APHE600
AILE649
AGLN654
AARG655
AARG656
AGLY657
ATYR658
AGLY659
AARG660
ASER684
ALEU686
ASER690
ASER693
ATYR694
AGLN760
AGOL803
AHOH934

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsZN_FING: C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000269|PubMed:22020126
ChainResidueDetails
ALEU537-TRP562

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:21217699, ECO:0000305|PubMed:27768893, ECO:0000305|PubMed:33657400
ChainResidueDetails
AGLU680

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:27382063, ECO:0000269|PubMed:29321206, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV, ECO:0007744|PDB:2PQ8, ECO:0007744|PDB:2Y0M, ECO:0007744|PDB:3QAH, ECO:0007744|PDB:3TOA, ECO:0007744|PDB:3TOB, ECO:0007744|PDB:4DNC, ECO:0007744|PDB:5J8C, ECO:0007744|PDB:5J8F, ECO:0007744|PDB:5WCI
ChainResidueDetails
ACYS540
ACYS543
AHIS556
ACYS560

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:29321206, ECO:0007744|PDB:5WCI
ChainResidueDetails
AILE647
AILE649
AARG655
AGLY659
AARG660
ASER684
ASER693

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV, ECO:0007744|PDB:2Y0M
ChainResidueDetails
AARG656
AGLY657

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0007744|PDB:2Y0M
ChainResidueDetails
ATYR738
ALYS762

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026, ECO:0000269|PubMed:22918831, ECO:0000269|PubMed:27382063, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV
ChainResidueDetails
AALY604

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER678

222624

PDB entries from 2024-07-17

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