Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6AQP

Aspergillus fumigatus Cytosolic Thiolase: Acetylated enzyme in complex with CoA and potassium ions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006694	biological_process	steroid biosynthetic process
A	0006696	biological_process	ergosterol biosynthetic process
A	0008202	biological_process	steroid metabolic process
A	0016126	biological_process	sterol biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0046872	molecular_function	metal ion binding
B	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006694	biological_process	steroid biosynthetic process
B	0006696	biological_process	ergosterol biosynthetic process
B	0008202	biological_process	steroid metabolic process
B	0016126	biological_process	sterol biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0046872	molecular_function	metal ion binding
C	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006629	biological_process	lipid metabolic process
C	0006694	biological_process	steroid biosynthetic process
C	0006696	biological_process	ergosterol biosynthetic process
C	0008202	biological_process	steroid metabolic process
C	0016126	biological_process	sterol biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0046872	molecular_function	metal ion binding
D	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0006694	biological_process	steroid biosynthetic process
D	0006696	biological_process	ergosterol biosynthetic process
D	0008202	biological_process	steroid metabolic process
D	0016126	biological_process	sterol biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue COA A 401

Chain	Residue
A	SCY92
A	SER253
A	ALA324
A	PHE325
A	HIS354
A	HOH519
A	HOH533
A	HOH538
A	HOH573
A	HOH594
A	HOH646
A	LEU152
A	HOH743
A	HOH752
A	TYR187
A	ASN227
A	LEU228
A	ASN229
A	LYS232
A	ALA249
A	PRO250

site_id	AC2
Number of Residues	6
Details	binding site for residue K A 402

Chain	Residue
A	TYR187
A	ALA249
A	PRO250
A	SER252
A	VAL350
A	HOH646

site_id	AC3
Number of Residues	5
Details	binding site for residue K A 403

Chain	Residue
A	LEU41
A	VAL44
A	LEU47
A	HOH662
A	HOH788

site_id	AC4
Number of Residues	6
Details	binding site for residue K A 404

Chain	Residue
A	ASP200
A	GLU201
A	ILE203
A	HOH787
A	HOH859
A	HOH860

site_id	AC5
Number of Residues	5
Details	binding site for residue CL A 405

Chain	Residue
A	ASN385
A	GLY389
A	HOH536
B	ARG71
B	HOH742

site_id	AC6
Number of Residues	21
Details	binding site for residue COA B 401

Chain	Residue
B	SCY92
B	LEU152
B	TYR187
B	ASN227
B	ASN229
B	LYS232
B	ILE236
B	PHE240
B	ALA249
B	PRO250
B	SER253
B	PHE294
B	ALA324
B	HIS354
B	HOH502
B	HOH524
B	HOH635
B	HOH640
B	HOH694
C	LYS137
C	HOH631

site_id	AC7
Number of Residues	6
Details	binding site for residue K B 402

Chain	Residue
B	TYR187
B	ALA249
B	PRO250
B	SER252
B	VAL350
B	HOH640

site_id	AC8
Number of Residues	6
Details	binding site for residue K B 403

Chain	Residue
B	ASP200
B	GLU201
B	ILE203
B	HOH618
B	HOH775
B	HOH813

site_id	AC9
Number of Residues	4
Details	binding site for residue K B 404

Chain	Residue
B	LEU41
B	VAL44
B	LEU47
B	HOH729

site_id	AD1
Number of Residues	5
Details	binding site for residue CL B 405

Chain	Residue
A	ARG71
A	HOH779
B	ASN385
B	GLY389
B	HOH504

site_id	AD2
Number of Residues	6
Details	binding site for residue K C 401

Chain	Residue
C	TYR187
C	ALA249
C	PRO250
C	SER252
C	VAL350
C	HOH743

site_id	AD3
Number of Residues	6
Details	binding site for residue K C 402

Chain	Residue
C	ASP200
C	GLU201
C	ILE203
C	HOH959
C	HOH996
C	HOH998

site_id	AD4
Number of Residues	6
Details	binding site for residue K C 403

Chain	Residue
C	LEU47
C	HOH817
C	HOH929
C	HOH937
C	LEU41
C	VAL44

site_id	AD5
Number of Residues	6
Details	binding site for residue CL C 404

Chain	Residue
C	ASN385
C	GLY387
C	GLY389
C	HOH544
D	ARG71
D	HOH876

site_id	AD6
Number of Residues	28
Details	binding site for residue ACO C 405

Chain	Residue
B	HOH657
C	SCY92
C	LEU152
C	MET161
C	TYR187
C	ASN227
C	ASN229
C	LYS232
C	LEU233
C	ILE236
C	ALA249
C	PRO250
C	SER253
C	PRO254
C	PHE294
C	ALA324
C	PHE325
C	HIS354
C	GLY386
C	HOH513
C	HOH515
C	HOH633
C	HOH724
C	HOH728
C	HOH734
C	HOH771
C	HOH773
C	HOH864

site_id	AD7
Number of Residues	27
Details	binding site for residue COA D 401

Chain	Residue
D	SCY92
D	LEU152
D	MET161
D	TYR187
D	ASN227
D	ASN229
D	LYS232
D	LEU233
D	ILE236
D	ALA249
D	PRO250
D	SER253
D	PRO254
D	PHE294
D	ALA324
D	PHE325
D	HOH512
D	HOH618
D	HOH659
D	HOH700
D	HOH726
D	HOH782
D	HOH792
D	HOH800
D	HOH818
D	HOH847
D	HOH858

site_id	AD8
Number of Residues	6
Details	binding site for residue K D 402

Chain	Residue
D	TYR187
D	ALA249
D	PRO250
D	SER252
D	VAL350
D	HOH700

site_id	AD9
Number of Residues	7
Details	binding site for residue K D 403

Chain	Residue
D	ASP200
D	GLU201
D	ILE203
D	HOH899
D	HOH977
D	HOH1002
D	HOH1061

site_id	AE1
Number of Residues	5
Details	binding site for residue K D 404

Chain	Residue
D	LEU41
D	VAL44
D	LEU47
D	HOH785
D	HOH907

site_id	AE2
Number of Residues	6
Details	binding site for residue CL D 405

Chain	Residue
C	ARG71
C	HOH816
D	ASN385
D	GLY387
D	GLY389
D	HOH621

Functional Information from PROSITE/UniProt

site_id	PS00053
Number of Residues	18
Details	RIBOSOMAL_S8 Ribosomal protein S8 signature. GarILTTLlGVLkakkGK

Chain	Residue	Details
A	GLY360-LYS377

site_id	PS00098
Number of Residues	19
Details	THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNKvCASGLkAIilgaqtI

Chain	Residue	Details
A	VAL88-ILE106

site_id	PS00737
Number of Residues	17
Details	THIOLASE_2 Thiolases signature 2. NlhGGaVAiGHPiGaSG

Chain	Residue	Details
A	ASN344-GLY360

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"UniProtKB","id":"P24752","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10020","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2018","firstPage":"1973","lastPage":"1989","volume":"8","journal":"ACS Catal.","title":"Structure of Aspergillus fumigatus cytosolic thiolase: trapped tetrahedral reaction intermediates and activation by monovalent cations.","authors":["Marshall A.C.","Bond C.S.","Bruning J.B."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.7b02873"}]}},{"source":"PDB","id":"6AQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ARF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ARG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ARL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ARR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ART","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2018","firstPage":"1973","lastPage":"1989","volume":"8","journal":"ACS Catal.","title":"Structure of Aspergillus fumigatus cytosolic thiolase: trapped tetrahedral reaction intermediates and activation by monovalent cations.","authors":["Marshall A.C.","Bond C.S.","Bruning J.B."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.7b02873"}]}},{"source":"PDB","id":"6ARE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)