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7XAY

Crystal structure of Hat1-Hat2-Asf1-H3-H4

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0005506molecular_functioniron ion binding
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
A0009055molecular_functionelectron transfer activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0031509biological_processsubtelomeric heterochromatin formation
A0042393molecular_functionhistone binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0000123cellular_componenthistone acetyltransferase complex
B0000781cellular_componentchromosome, telomeric region
B0004402molecular_functionhistone acetyltransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0006355biological_processregulation of DNA-templated transcription
B0031509biological_processsubtelomeric heterochromatin formation
B0033698cellular_componentRpd3L complex
B0042393molecular_functionhistone binding
B0070210cellular_componentRpd3L-Expanded complex
C0005634cellular_componentnucleus
C0006325biological_processchromatin organization
D0000500cellular_componentRNA polymerase I upstream activating factor complex
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0006325biological_processchromatin organization
D0006355biological_processregulation of DNA-templated transcription
D0006878biological_processintracellular copper ion homeostasis
D0008823molecular_functioncupric reductase activity
D0009060biological_processaerobic respiration
D0009303biological_processrRNA transcription
D0030527molecular_functionstructural constituent of chromatin
D0031298cellular_componentreplication fork protection complex
D0032991cellular_componentprotein-containing complex
D0042790biological_processnucleolar large rRNA transcription by RNA polymerase I
D0043505cellular_componentCENP-A containing nucleosome
D0043935biological_processsexual sporulation resulting in formation of a cellular spore
D0045943biological_processpositive regulation of transcription by RNA polymerase I
D0046982molecular_functionprotein heterodimerization activity
D0070911biological_processglobal genome nucleotide-excision repair
E0000500cellular_componentRNA polymerase I upstream activating factor complex
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0006355biological_processregulation of DNA-templated transcription
E0030527molecular_functionstructural constituent of chromatin
E0031298cellular_componentreplication fork protection complex
E0032991cellular_componentprotein-containing complex
E0042790biological_processnucleolar large rRNA transcription by RNA polymerase I
E0045943biological_processpositive regulation of transcription by RNA polymerase I
E0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
EGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
DLYS14-LEU20

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
DPRO66-ILE74

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSGsdDhTVALWEV
ChainResidueDetails
BLEU176-VAL190
BVAL311-LEU325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsDNA_BIND:
ChainResidueDetails
ELYS16-LYS20
AILE6

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:22343720
ChainResidueDetails
ELYS8
DLYS27
ELYS12

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11080160, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592, ECO:0000269|PubMed:19113941
ChainResidueDetails
AGLN227
AASN258
ELYS16

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435
ChainResidueDetails
ELYS77
ELYS31

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000269|PubMed:19113941
ChainResidueDetails
EARG55
DLYS56

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ESER60

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:19779198
ChainResidueDetails
ESER64

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:16768447
ChainResidueDetails
ELYS79

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-glutaryllysine => ECO:0000269|PubMed:31542297
ChainResidueDetails
ELYS91

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 224
ChainResidueDetails
APHE220electrostatic stabiliser, hydrogen bond donor
AGLU255hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

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