Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6ARE

Aspergillus fumigatus Cytosolic Thiolase in complex with two tetrahedral reaction intermediates and ammonium 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	23
Details	binding site for residue COA A 401

Chain	Residue
A	SCY92
A	PRO250
A	SER253
A	PHE294
A	ALA324
A	PHE325
A	HIS354
A	HOH519
A	HOH599
A	HOH610
A	HOH615
A	LEU152
A	HOH686
A	HOH690
A	HOH747
A	HOH778
A	TYR187
A	ASN227
A	LEU228
A	ASN229
A	LYS232
A	ILE236
A	ALA249

site_id	AC2
Number of Residues	5
Details	binding site for residue CL A 402

Chain	Residue
A	ASN385
A	GLY389
A	HOH611
B	ARG71
B	HOH798

site_id	AC3
Number of Residues	6
Details	binding site for residue NH4 A 403

Chain	Residue
A	TYR187
A	ALA249
A	PRO250
A	SER252
A	VAL350
A	HOH690

site_id	AC4
Number of Residues	5
Details	binding site for residue NH4 A 404

Chain	Residue
A	ASP200
A	GLU201
A	ILE203
A	HOH535
A	HOH703

site_id	AC5
Number of Residues	19
Details	binding site for residue COA B 401

Chain	Residue
B	SCY92
B	LEU152
B	MET161
B	TYR187
B	ASN227
B	ASN229
B	LYS232
B	LEU233
B	ILE236
B	ALA249
B	PRO250
B	SER253
B	ALA324
B	HIS354
B	HOH505
B	HOH601
B	HOH670
B	HOH730
B	HOH746

site_id	AC6
Number of Residues	6
Details	binding site for residue CL B 402

Chain	Residue
A	ARG71
A	HOH738
B	ASN385
B	GLY387
B	GLY389
B	HOH603

site_id	AC7
Number of Residues	6
Details	binding site for residue NH4 B 403

Chain	Residue
B	TYR187
B	ALA249
B	PRO250
B	SER252
B	VAL350
B	HOH670

site_id	AC8
Number of Residues	4
Details	binding site for residue NH4 B 404

Chain	Residue
B	ASP200
B	GLU201
B	ILE203
B	HOH748

site_id	AC9
Number of Residues	2
Details	binding site for residue NH4 B 405

Chain	Residue
B	VAL44
B	LEU47

site_id	AD1
Number of Residues	5
Details	binding site for residue CL C 402

Chain	Residue
C	ASN385
C	GLY389
C	HOH536
D	ARG71
D	HOH656

site_id	AD2
Number of Residues	6
Details	binding site for residue NH4 C 403

Chain	Residue
C	TYR187
C	ALA249
C	PRO250
C	SER252
C	VAL350
C	HOH645

site_id	AD3
Number of Residues	4
Details	binding site for residue NH4 C 404

Chain	Residue
C	ASP200
C	GLU201
C	ILE203
C	HOH667

site_id	AD4
Number of Residues	3
Details	binding site for residue NH4 C 405

Chain	Residue
C	LEU41
C	VAL44
C	LEU47

site_id	AD5
Number of Residues	14
Details	binding site for residue COA D 401

Chain	Residue
D	ASN229
D	ILE236
D	PRO250
D	SER253
D	ALA324
D	HIS354
D	ACT402
D	HOH506
D	HOH585
D	CYS92
D	LEU152
D	MET161
D	TYR187
D	ASN227

site_id	AD6
Number of Residues	5
Details	binding site for residue CL D 403

Chain	Residue
C	ARG71
C	HOH670
D	ASN385
D	GLY389
D	HOH515

site_id	AD7
Number of Residues	6
Details	binding site for residue NH4 D 404

Chain	Residue
D	TYR187
D	ALA249
D	PRO250
D	SER252
D	VAL350
D	HOH585

site_id	AD8
Number of Residues	4
Details	binding site for residue NH4 D 405

Chain	Residue
D	ASP200
D	GLU201
D	ILE203
D	HOH578

site_id	AD9
Number of Residues	13
Details	binding site for Di-peptide ACT C 401 and CYS C 92

Chain	Residue
C	LYS90
C	VAL91
C	ALA93
C	SER94
C	GLY151
C	HIS354
C	ILE356
C	ILE383
C	CYS384
C	ASN385
C	GLY386
C	ACO406
C	HOH514

site_id	AE1
Number of Residues	21
Details	binding site for residues ACT C 401 and ACO C 406

Chain	Residue
C	VAL91
C	CYS92
C	GLY151
C	LEU152
C	TYR187
C	ASN227
C	LEU228
C	ASN229
C	ILE236
C	PHE240
C	ALA249
C	SER253
C	ALA324
C	PHE325
C	HIS354
C	CYS384
C	ASN385
C	GLY386
C	HOH501
C	HOH533
C	HOH575

site_id	AE2
Number of Residues	14
Details	binding site for Di-peptide ACT D 402 and CYS D 92

Chain	Residue
C	GLN67
D	LYS90
D	VAL91
D	ALA93
D	SER94
D	GLY151
D	HIS354
D	ILE356
D	ILE383
D	CYS384
D	ASN385
D	GLY386
D	COA401
D	HOH512

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	GLY360-LYS377
A	GLY360-LYS377

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

Chain	Residue	Details
C	VAL88-ILE106
A	VAL88-ILE106

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

Chain	Residue	Details
C	ASN344-GLY360
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)