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6QGQ

Crystal structure of APT1 C2S mutant bound to palmitic acid.

Functional Information from GO Data
ChainGOidnamespacecontents
A0002084biological_processprotein depalmitoylation
A0004620molecular_functionphospholipase activity
A0004622molecular_functionphosphatidylcholine lysophospholipase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0008474molecular_functionpalmitoyl-(protein) hydrolase activity
A0015908biological_processfatty acid transport
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
A0031965cellular_componentnuclear membrane
A0042997biological_processnegative regulation of Golgi to plasma membrane protein transport
A0070062cellular_componentextracellular exosome
A1905336biological_processnegative regulation of aggrephagy
B0002084biological_processprotein depalmitoylation
B0004620molecular_functionphospholipase activity
B0004622molecular_functionphosphatidylcholine lysophospholipase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0008474molecular_functionpalmitoyl-(protein) hydrolase activity
B0015908biological_processfatty acid transport
B0016298molecular_functionlipase activity
B0016787molecular_functionhydrolase activity
B0031965cellular_componentnuclear membrane
B0042997biological_processnegative regulation of Golgi to plasma membrane protein transport
B0070062cellular_componentextracellular exosome
B1905336biological_processnegative regulation of aggrephagy
C0002084biological_processprotein depalmitoylation
C0004620molecular_functionphospholipase activity
C0004622molecular_functionphosphatidylcholine lysophospholipase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005783cellular_componentendoplasmic reticulum
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0008474molecular_functionpalmitoyl-(protein) hydrolase activity
C0015908biological_processfatty acid transport
C0016298molecular_functionlipase activity
C0016787molecular_functionhydrolase activity
C0031965cellular_componentnuclear membrane
C0042997biological_processnegative regulation of Golgi to plasma membrane protein transport
C0070062cellular_componentextracellular exosome
C1905336biological_processnegative regulation of aggrephagy
D0002084biological_processprotein depalmitoylation
D0004620molecular_functionphospholipase activity
D0004622molecular_functionphosphatidylcholine lysophospholipase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005783cellular_componentendoplasmic reticulum
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0008474molecular_functionpalmitoyl-(protein) hydrolase activity
D0015908biological_processfatty acid transport
D0016298molecular_functionlipase activity
D0016787molecular_functionhydrolase activity
D0031965cellular_componentnuclear membrane
D0042997biological_processnegative regulation of Golgi to plasma membrane protein transport
D0070062cellular_componentextracellular exosome
D1905336biological_processnegative regulation of aggrephagy
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue GOL A 301
ChainResidue
ATRP37
BMET65

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 302
ChainResidue
AMET65
AHOH403
BGLY36

site_idAC3
Number of Residues9
Detailsbinding site for residue PLM B 401
ChainResidue
BTRP145
BARG149
BPHE181
BTHR185
BHOH505
BLEU30
BLEU78
BSER119
BGLN120

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL C 601
ChainResidue
CASP32
CGLY36
CTRP37
CSER210
CHOH722

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL D 301
ChainResidue
CMET65
DASP32
DGLY36
DTRP37
DSER210
DHOH402

site_idAC6
Number of Residues11
Detailsbinding site for residue PLM D 302
ChainResidue
DLEU30
DILE75
DGLY77
DLEU78
DSER79
DSER119
DGLN120
DTRP145
DVAL177
DPHE181
DHOH407

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"19439193","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37802024","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11080636","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97823","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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