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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6PW9

Cryo-EM structure of human NatE/HYPK complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004596molecular_functionprotein-N-terminal amino-acid acetyltransferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006474biological_processN-terminal protein amino acid acetylation
A0007064biological_processmitotic sister chromatid cohesion
A0010485molecular_functionhistone H4 acetyltransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0031415cellular_componentNatA complex
A0034087biological_processestablishment of mitotic sister chromatid cohesion
A0043687biological_processpost-translational protein modification
A0061733molecular_functionprotein-lysine-acetyltransferase activity
A0070062cellular_componentextracellular exosome
A0071962biological_processmitotic sister chromatid cohesion, centromeric
A0120518molecular_functionprotein N-terminal-methionine acetyltransferase activity
B0001525biological_processangiogenesis
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005667cellular_componenttranscription regulator complex
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006474biological_processN-terminal protein amino acid acetylation
B0010698molecular_functionacetyltransferase activator activity
B0016020cellular_componentmembrane
B0016407molecular_functionacetyltransferase activity
B0016604cellular_componentnuclear body
B0030154biological_processcell differentiation
B0031415cellular_componentNatA complex
B0043022molecular_functionribosome binding
B0043066biological_processnegative regulation of apoptotic process
B0045893biological_processpositive regulation of DNA-templated transcription
B0050821biological_processprotein stabilization
C0004596molecular_functionprotein-N-terminal amino-acid acetyltransferase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006473biological_processprotein acetylation
C0006474biological_processN-terminal protein amino acid acetylation
C0006475biological_processinternal protein amino acid acetylation
C0008080molecular_functionN-acetyltransferase activity
C0008999molecular_functionprotein-N-terminal-alanine acetyltransferase activity
C0016020cellular_componentmembrane
C0016407molecular_functionacetyltransferase activity
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0031415cellular_componentNatA complex
C0043022molecular_functionribosome binding
C0051276biological_processchromosome organization
C1990189molecular_functionprotein N-terminal-serine acetyltransferase activity
C1990190molecular_functionprotein-N-terminal-glutamate acetyltransferase activity
C2000719biological_processnegative regulation of maintenance of mitotic sister chromatid cohesion, centromeric
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0006457biological_processprotein folding
D0015630cellular_componentmicrotubule cytoskeleton
D0032991cellular_componentprotein-containing complex
D0043066biological_processnegative regulation of apoptotic process
D0044183molecular_functionprotein folding chaperone
D0050821biological_processprotein stabilization
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue IHP C 901
ChainResidue
BLYS419
BLYS447
BTYR451
BLYS556
CHIS16
CLEU20
CLYS51
CLYS78
site_idAC2
Number of Residues17
Detailsbinding site for residue ACO C 902
ChainResidue
AASP53
CLEU22
CTHR73
CLEU75
CVAL77
CARG82
CARG83
CGLY85
CLEU86
CALA87
CHIS110
CALA117
CHIS120
CLEU121
CTYR122
CTHR125
AARG5
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues300
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27484799","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X5K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27484799","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2007","submissionDatabase":"PDB data bank","title":"Structure of human MAK3 homolog.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2PSW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X5K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues36
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues33
DetailsRepeat: {"description":"TPR 4"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues33
DetailsRepeat: {"description":"TPR 5"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues32
DetailsRepeat: {"description":"TPR 6"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues33
DetailsRepeat: {"description":"TPR 7"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues33
DetailsRepeat: {"description":"TPR 8"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues57
DetailsRegion: {"description":"Interaction with NAA15","evidences":[{"source":"PubMed","id":"15496142","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"27708256","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues69
DetailsRegion: {"description":"Required for association with the NAA10-NAA15 complex","evidences":[{"source":"PubMed","id":"29754825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues45
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues15
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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