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 | 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 | 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 | 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 |
