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6ARF

Aspergillus fumigatus Cytosolic Thiolase: Apo enzyme in complex with potassium ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006696biological_processergosterol biosynthetic process
A0016126biological_processsterol biosynthetic process
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0046872molecular_functionmetal ion binding
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006696biological_processergosterol biosynthetic process
B0016126biological_processsterol biosynthetic process
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0046872molecular_functionmetal ion binding
C0003985molecular_functionacetyl-CoA C-acetyltransferase activity
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006696biological_processergosterol biosynthetic process
C0016126biological_processsterol biosynthetic process
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0046872molecular_functionmetal ion binding
D0003985molecular_functionacetyl-CoA C-acetyltransferase activity
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0006696biological_processergosterol biosynthetic process
D0016126biological_processsterol biosynthetic process
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CL A 401
ChainResidue
AASN385
AGLY387
AGLY389
BARG71
BHOH579
BHOH649

site_idAC2
Number of Residues6
Detailsbinding site for residue K A 402
ChainResidue
ASER252
AVAL350
AHOH576
ATYR187
AALA249
APRO250

site_idAC3
Number of Residues5
Detailsbinding site for residue K A 403
ChainResidue
ALEU41
AVAL44
ALEU47
AHOH620
AHOH632

site_idAC4
Number of Residues5
Detailsbinding site for residue K A 404
ChainResidue
AASP200
AGLU201
AILE203
AHOH643
AHOH650

site_idAC5
Number of Residues5
Detailsbinding site for residue CL B 401
ChainResidue
AARG71
AHOH608
BASN385
BGLY387
BGLY389

site_idAC6
Number of Residues6
Detailsbinding site for residue K B 402
ChainResidue
BTYR187
BALA249
BPRO250
BSER252
BVAL350
BHOH628

site_idAC7
Number of Residues4
Detailsbinding site for residue K B 403
ChainResidue
BASP200
BGLU201
BILE203
BHOH662

site_idAC8
Number of Residues4
Detailsbinding site for residue K B 404
ChainResidue
BLEU41
BVAL44
BLEU47
BHOH658

site_idAC9
Number of Residues5
Detailsbinding site for residue CL C 401
ChainResidue
CASN385
CGLY389
CHOH683
DARG71
DHOH789

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL C 402
ChainResidue
CASN227
CLEU228
CASN229
CLYS232
CHOH589
CHOH796

site_idAD2
Number of Residues7
Detailsbinding site for residue GOL C 403
ChainResidue
CLEU27
CHIS35
CGLN207
CHOH670
CHOH730
CHOH811
CHOH814

site_idAD3
Number of Residues6
Detailsbinding site for residue K C 404
ChainResidue
CTYR187
CALA249
CPRO250
CSER252
CVAL350
CHOH843

site_idAD4
Number of Residues5
Detailsbinding site for residue K C 405
ChainResidue
CASP200
CGLU201
CILE203
CHOH910
CHOH942

site_idAD5
Number of Residues5
Detailsbinding site for residue K C 406
ChainResidue
CLEU41
CVAL44
CLEU47
CHOH630
CHOH882

site_idAD6
Number of Residues6
Detailsbinding site for residue CL D 401
ChainResidue
CARG71
CHOH759
DASN385
DGLY387
DGLY389
DHOH619

site_idAD7
Number of Residues7
Detailsbinding site for residue GOL D 402
ChainResidue
DASN227
DASN229
DLYS232
DLEU233
DHOH553
DHOH685
DHOH737

site_idAD8
Number of Residues6
Detailsbinding site for residue GOL D 403
ChainResidue
DHIS35
DGLN207
DHOH503
DHOH513
DHOH632
DHOH723

site_idAD9
Number of Residues3
Detailsbinding site for residue GOL D 404
ChainResidue
DARG185
DGLU341
DHOH623

site_idAE1
Number of Residues6
Detailsbinding site for residue K D 405
ChainResidue
DPRO250
DSER252
DVAL350
DHOH835
DTYR187
DALA249

site_idAE2
Number of Residues7
Detailsbinding site for residue K D 406
ChainResidue
DASP200
DGLU201
DILE203
DHOH857
DHOH870
DHOH955
DHOH965

site_idAE3
Number of Residues6
Detailsbinding site for residue K D 407
ChainResidue
DLEU41
DVAL44
DLEU47
DHOH647
DHOH875
DHOH894

site_idAE4
Number of Residues3
Detailsbinding site for residue K D 408
ChainResidue
DASP45
DLEU273
DASN274

Functional Information from PROSITE/UniProt
site_idPS00053
Number of Residues18
DetailsRIBOSOMAL_S8 Ribosomal protein S8 signature. GarILTTLlGVLkakkGK
ChainResidueDetails
AGLY360-LYS377

site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNKvCASGLkAIilgaqtI
ChainResidueDetails
AVAL88-ILE106

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NlhGGaVAiGHPiGaSG
ChainResidueDetails
AASN344-GLY360

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000250|UniProtKB:P24752
ChainResidueDetails
ACYS92
BCYS92
CCYS92
DCYS92

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020
ChainResidueDetails
AHIS354
ACYS384
BHIS354
BCYS384
CHIS354
CCYS384
DHIS354
DCYS384

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|DOI:10.1021/acscatal.7b02873, ECO:0007744|PDB:6AQP, ECO:0007744|PDB:6ARF, ECO:0007744|PDB:6ARG, ECO:0007744|PDB:6ARL, ECO:0007744|PDB:6ARR, ECO:0007744|PDB:6ART
ChainResidueDetails
ATYR187
BSER252
BVAL350
BASN385
CTYR187
CALA249
CPRO250
CSER252
CVAL350
CASN385
DTYR187
AALA249
DALA249
DPRO250
DSER252
DVAL350
DASN385
APRO250
ASER252
AVAL350
AASN385
BTYR187
BALA249
BPRO250

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|DOI:10.1021/acscatal.7b02873, ECO:0007744|PDB:6ARE
ChainResidueDetails
AASN229
DASN229
DLYS232
DSER253
ALYS232
ASER253
BASN229
BLYS232
BSER253
CASN229
CLYS232
CSER253

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PDB entries from 2024-11-06

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