6ARL
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 | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0006696 | biological_process | ergosterol biosynthetic process |
A | 0016126 | biological_process | sterol biosynthetic process |
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 | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0006696 | biological_process | ergosterol biosynthetic process |
B | 0016126 | biological_process | sterol biosynthetic process |
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 | 0006635 | biological_process | fatty acid beta-oxidation |
C | 0006696 | biological_process | ergosterol biosynthetic process |
C | 0016126 | biological_process | sterol biosynthetic process |
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 | 0006635 | biological_process | fatty acid beta-oxidation |
D | 0006696 | biological_process | ergosterol biosynthetic process |
D | 0016126 | biological_process | sterol biosynthetic process |
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 | 3 |
Details | binding site for residue RB A 401 |
Chain | Residue |
A | LEU41 |
A | VAL44 |
A | LEU47 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue RB A 402 |
Chain | Residue |
A | ASP200 |
A | GLU201 |
A | ILE203 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue RB A 403 |
Chain | Residue |
A | SER252 |
A | VAL350 |
A | TYR187 |
A | ALA249 |
A | PRO250 |
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 | HOH590 |
B | HOH647 |
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 | HOH665 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CL B 404 |
Chain | Residue |
A | ARG71 |
A | HOH621 |
B | ASN385 |
B | GLY387 |
B | GLY389 |
B | HOH568 |
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 | HOH820 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue RB C 402 |
Chain | Residue |
C | ASP200 |
C | GLU201 |
C | ILE203 |
C | HOH874 |
C | HOH881 |
C | HOH892 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue RB C 403 |
Chain | Residue |
C | LEU41 |
C | VAL44 |
C | LEU47 |
C | HOH845 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue GOL C 404 |
Chain | Residue |
C | ASN227 |
C | ASN229 |
C | LEU233 |
C | ILE236 |
C | PRO250 |
C | HOH533 |
C | HOH655 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue CL C 405 |
Chain | Residue |
C | ASN385 |
C | GLY387 |
C | GLY389 |
C | HOH604 |
D | ARG71 |
D | HOH729 |
site_id | AD5 |
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 | HOH653 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue RB D 402 |
Chain | Residue |
D | ASP200 |
D | GLU201 |
D | ILE203 |
D | HOH816 |
D | HOH919 |
D | HOH920 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue RB D 403 |
Chain | Residue |
D | LEU41 |
D | VAL44 |
D | LEU47 |
D | HOH703 |
D | HOH838 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue RB D 404 |
Chain | Residue |
D | ASP45 |
D | LEU273 |
D | ASN274 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue GOL D 405 |
Chain | Residue |
D | LEU21 |
D | GLY22 |
D | SER25 |
D | HOH511 |
D | HOH646 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue GOL D 406 |
Chain | Residue |
D | ASN227 |
D | ASN229 |
D | LYS232 |
D | HOH577 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue CL D 407 |
Chain | Residue |
C | ARG71 |
C | HOH788 |
D | ASN385 |
D | GLY389 |
D | HOH586 |
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 | ACT_SITE: Acyl-thioester intermediate => ECO:0000250|UniProtKB:P24752 |
Chain | Residue | Details |
A | CYS92 | |
B | CYS92 | |
C | CYS92 | |
D | CYS92 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020 |
Chain | Residue | Details |
A | HIS354 | |
A | CYS384 | |
B | HIS354 | |
B | CYS384 | |
C | HIS354 | |
C | CYS384 | |
D | HIS354 | |
D | CYS384 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | TYR187 | |
B | SER252 | |
B | VAL350 | |
B | ASN385 | |
C | TYR187 | |
C | ALA249 | |
C | PRO250 | |
C | SER252 | |
C | VAL350 | |
C | ASN385 | |
D | TYR187 | |
A | ALA249 | |
D | ALA249 | |
D | PRO250 | |
D | SER252 | |
D | VAL350 | |
D | ASN385 | |
A | PRO250 | |
A | SER252 | |
A | VAL350 | |
A | ASN385 | |
B | TYR187 | |
B | ALA249 | |
B | PRO250 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|DOI:10.1021/acscatal.7b02873, ECO:0007744|PDB:6ARE |
Chain | Residue | Details |
A | ASN229 | |
D | ASN229 | |
D | LYS232 | |
D | SER253 | |
A | LYS232 | |
A | SER253 | |
B | ASN229 | |
B | LYS232 | |
B | SER253 | |
C | ASN229 | |
C | LYS232 | |
C | SER253 |