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4XPD

Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) in complex with a bisubstrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004596molecular_functionprotein-N-terminal amino-acid acetyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0010698molecular_functionacetyltransferase activator activity
A0031415cellular_componentNatA complex
A0043022molecular_functionribosome binding
B0004596molecular_functionprotein-N-terminal amino-acid acetyltransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006474biological_processN-terminal protein amino acid acetylation
B0008999molecular_functionprotein-N-terminal-alanine acetyltransferase activity
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0031415cellular_componentNatA complex
B0042802molecular_functionidentical protein binding
B1990189molecular_functionprotein N-terminal-serine acetyltransferase activity
B1990190molecular_functionprotein-N-terminal-glutamate acetyltransferase activity
C0004596molecular_functionprotein-N-terminal amino-acid acetyltransferase activity
C0005737cellular_componentcytoplasm
C0007064biological_processmitotic sister chromatid cohesion
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0031415cellular_componentNatA complex
C0120518molecular_functionprotein N-terminal-methionine acetyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue G4P A 901
ChainResidue
AGLN353
AARG426
ALYS429
ALYS457
ALYS460
ATYR461
BPRO83
BTYR85
BLYS91

site_idAC2
Number of Residues17
Detailsbinding site for residue ACO C 201
ChainResidue
AGLN320
CVAL27
CTYR31
CILE93
CGLU94
CLEU96
CARG103
CHIS104
CLYS105
CSER106
CILE107
CGLY108
CSER109
CVAL129
CTYR130
CLEU131
CTRP141

site_idAC3
Number of Residues21
Detailsbinding site for residue CMC F 101
ChainResidue
BASN23
BLEU24
BSER117
BLEU118
BSER119
BVAL120
BARG125
BARG126
BMET127
BGLY128
BILE129
BALA130
BGLU131
BHIS153
BASN158
BALA160
BHIS163
BTYR165
BTHR168
CGLU68
FSER1

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues33
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsRepeat: {"description":"TPR 4"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues33
DetailsRepeat: {"description":"TPR 5"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues33
DetailsRepeat: {"description":"TPR 6"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues33
DetailsRepeat: {"description":"TPR 7"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues33
DetailsRepeat: {"description":"TPR 8"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine; in Corticotropin","evidences":[{"source":"UniProtKB","id":"P01191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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