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3TOA

Human MOF crystal structure with active site lysine partially acetylated

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 501
ChainResidue
ACYS210
ACYS213
AHIS226
ACYS230

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 502
ChainResidue
AASP190

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AHIS226
AASP190
AALA191
ASER222
APHE225

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
ALEU318
ATHR319
AGLN324
ASER354
ALEU356

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
ALYS306
AGLU307
AGLU343

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
ALEU207-TRP232

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000303|PubMed:21217699, ECO:0000303|PubMed:22020126, ECO:0000305
ChainResidueDetails
AGLU350

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23
ChainResidueDetails
AILE317
AGLN324
ASER354
ASER363
ALYS432

site_idSWS_FT_FI4
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|Ref.23
ChainResidueDetails
AALY274

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER348

218853

PDB entries from 2024-04-24

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