Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6ARG

Aspergillus fumigatus Cytosolic Thiolase: Apo enzyme in complex with rubidium 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	5
Details	binding site for residue RB A 401

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

site_id	AC2
Number of Residues	3
Details	binding site for residue RB A 402

Chain	Residue
A	LEU41
A	VAL44
A	LEU47

site_id	AC3
Number of Residues	4
Details	binding site for residue RB A 403

Chain	Residue
A	GLU201
A	ILE203
A	HOH684
A	ASP200

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

Chain	Residue
A	ASN385
A	GLY387
A	GLY389
B	ARG71
B	HOH609
B	HOH655

site_id	AC5
Number of Residues	5
Details	binding site for residue RB B 401

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

site_id	AC6
Number of Residues	3
Details	binding site for residue RB B 402

Chain	Residue
B	ASP200
B	GLU201
B	ILE203

site_id	AC7
Number of Residues	4
Details	binding site for residue RB B 403

Chain	Residue
B	LEU41
B	VAL44
B	LEU47
B	HOH685

site_id	AC8
Number of Residues	6
Details	binding site for residue CL B 404

Chain	Residue
A	ARG71
A	HOH647
B	ASN385
B	GLY387
B	GLY389
B	HOH607

site_id	AC9
Number of Residues	6
Details	binding site for residue RB C 401

Chain	Residue
C	TYR187
C	ALA249
C	PRO250
C	SER252
C	VAL350
C	HOH858

site_id	AD1
Number of Residues	7
Details	binding site for residue RB C 402

Chain	Residue
C	ASP200
C	GLU201
C	ILE203
C	HOH822
C	HOH885
C	HOH914
C	HOH971

site_id	AD2
Number of Residues	4
Details	binding site for residue RB C 403

Chain	Residue
C	LEU41
C	VAL44
C	LEU47
C	HOH849

site_id	AD3
Number of Residues	6
Details	binding site for residue CL C 404

Chain	Residue
C	ASN385
C	GLY387
C	GLY389
C	HOH627
D	ARG71
D	HOH741

site_id	AD4
Number of Residues	7
Details	binding site for residue GOL C 405

Chain	Residue
C	ASN227
C	ASN229
C	LYS232
C	LEU233
C	ILE236
C	PRO250
C	HOH570

site_id	AD5
Number of Residues	5
Details	binding site for residue GOL C 406

Chain	Residue
C	SER50
C	ASP51
C	HOH523
C	HOH560
C	HOH809

site_id	AD6
Number of Residues	6
Details	binding site for residue RB D 401

Chain	Residue
D	TYR187
D	ALA249
D	PRO250
D	SER252
D	VAL350
D	HOH886

site_id	AD7
Number of Residues	5
Details	binding site for residue RB D 402

Chain	Residue
D	ASP200
D	GLU201
D	ILE203
D	HOH941
D	HOH978

site_id	AD8
Number of Residues	6
Details	binding site for residue RB D 403

Chain	Residue
D	LEU41
D	VAL44
D	LEU47
D	HOH736
D	HOH881
D	HOH1021

site_id	AD9
Number of Residues	3
Details	binding site for residue RB D 404

Chain	Residue
D	ASP45
D	LEU273
D	ASN274

site_id	AE1
Number of Residues	6
Details	binding site for residue CL D 405

Chain	Residue
C	ARG71
C	HOH790
D	ASN385
D	GLY387
D	GLY389
D	HOH568

site_id	AE2
Number of Residues	6
Details	binding site for residue GOL D 406

Chain	Residue
D	ASN229
D	LYS232
D	LEU233
D	HOH590
D	ASN227
D	LEU228

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)