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6VO5

Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4

Replaces:  6UHD
Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
A0031509biological_processsubtelomeric heterochromatin formation
A0042393molecular_functionhistone binding
B0004402molecular_functionhistone acetyltransferase activity
B0005634cellular_componentnucleus
B0006325biological_processchromatin organization
B0031509biological_processsubtelomeric heterochromatin formation
B0042393molecular_functionhistone binding
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue ACT A 501
ChainResidue
AARG39
APHE247
AHOH835

site_idAC2
Number of Residues25
Detailsbinding site for residue CO6 A 502
ChainResidue
AGLN248
AGLY249
AGLN250
AGLY251
AHIS252
AGLY253
AALA254
AALA275
APRO278
ASER279
ASER281
ATYR282
ALYS284
ALEU285
APHE288
AHOH627
AHOH644
AHOH673
AHOH864
APHE185
AILE186
AVAL238
AMET241
ALEU242
AILE243

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 503
ChainResidue
AASP196
AHOH610
AHOH634
AHOH674
BASP193
BASP195
CLYS8

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 504
ChainResidue
ATHR274
AALA275
APRO278
AARG286
AGLN326
AHIS327

site_idAC5
Number of Residues31
Detailsbinding site for residue CO6 B 401
ChainResidue
BPHE185
BILE186
BVAL238
BSER239
BGLN240
BMET241
BLEU242
BILE243
BGLN248
BGLY249
BGLN250
BGLY251
BHIS252
BGLY253
BALA254
BGLU276
BASP277
BPRO278
BSER279
BSER281
BTYR282
BLYS284
BLEU285
BPHE288
BHOH531
BHOH556
BHOH571
BHOH572
BHOH578
BHOH628
BHOH758

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL B 402
ChainResidue
BLEU143
BHIS144
BTHR145

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL B 403
ChainResidue
BGLY140
BTHR141
BLYS163
BALA164
BASP165
BHOH587
BHOH658

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 B 404
ChainResidue
BTHR274
BALA275
BPRO278
BARG286
BHIS327
BHOH623

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
CGLY14-HIS18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsDNA_BIND:
ChainResidueDetails
CLYS16-LYS20
DLYS16-LYS20

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17967882
ChainResidueDetails
CSER1
DSER1
BMET241
BGLN248

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
CARG3
DARG3

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
CLYS5
DLYS5

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393
ChainResidueDetails
CLYS8
CLYS16
DLYS8
DLYS16

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
CALA12
DALA12

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793
ChainResidueDetails
CLYS20
DLYS20

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447
ChainResidueDetails
CALA12
DALA12

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS20
DLYS20

219140

PDB entries from 2024-05-01

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