2D3T
Fatty Acid beta-oxidation multienzyme complex from Pseudomonas Fragi, Form V
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
A | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0008692 | molecular_function | 3-hydroxybutyryl-CoA epimerase activity |
A | 0009062 | biological_process | fatty acid catabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0016829 | molecular_function | lyase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0036125 | cellular_component | fatty acid beta-oxidation multienzyme complex |
A | 0044248 | biological_process | cellular catabolic process |
A | 0070403 | molecular_function | NAD+ binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
B | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
B | 0004300 | molecular_function | enoyl-CoA hydratase activity |
B | 0005515 | molecular_function | protein binding |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0008692 | molecular_function | 3-hydroxybutyryl-CoA epimerase activity |
B | 0009062 | biological_process | fatty acid catabolic process |
B | 0016042 | biological_process | lipid catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0016829 | molecular_function | lyase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0036125 | cellular_component | fatty acid beta-oxidation multienzyme complex |
B | 0044248 | biological_process | cellular catabolic process |
B | 0070403 | molecular_function | NAD+ binding |
C | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006635 | biological_process | fatty acid beta-oxidation |
C | 0016042 | biological_process | lipid catabolic process |
C | 0016746 | molecular_function | acyltransferase activity |
C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
D | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006631 | biological_process | fatty acid metabolic process |
D | 0006635 | biological_process | fatty acid beta-oxidation |
D | 0016042 | biological_process | lipid catabolic process |
D | 0016746 | molecular_function | acyltransferase activity |
D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ACO C 1003 |
Chain | Residue |
C | CYS95 |
C | ILE245 |
C | MET284 |
C | ASN312 |
C | ALA314 |
C | HIS347 |
C | CYS377 |
C | MET151 |
C | HIS177 |
C | ARG215 |
C | LEU223 |
C | PHE230 |
C | ALA239 |
C | GLY240 |
C | SER243 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ACO D 1004 |
Chain | Residue |
D | CYS95 |
D | MET151 |
D | ARG215 |
D | THR218 |
D | SER222 |
D | LEU223 |
D | LEU226 |
D | PHE230 |
D | SER243 |
D | MET284 |
D | ASN312 |
D | ALA314 |
D | PHE315 |
D | HIS347 |
D | CYS377 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE NAD A 1001 |
Chain | Residue |
A | ALA322 |
A | ILE324 |
A | MET325 |
A | LYS343 |
A | ASP344 |
A | ASN346 |
A | GLY349 |
A | ALA400 |
A | VAL401 |
A | GLU403 |
A | VAL411 |
A | ASN428 |
A | THR429 |
A | SER430 |
A | ASN454 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NAD B 1002 |
Chain | Residue |
B | ALA322 |
B | ILE324 |
B | MET325 |
B | ASP344 |
B | ILE345 |
B | ALA400 |
B | VAL401 |
B | GLU403 |
B | VAL411 |
B | ASN428 |
B | THR429 |
B | SER430 |
B | ASN454 |
Functional Information from PROSITE/UniProt
site_id | PS00067 |
Number of Residues | 25 |
Details | 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DcpGFLvNRvlfPYFggfak.LVsaG |
Chain | Residue | Details |
A | ASP494-GLY518 |
site_id | PS00098 |
Number of Residues | 19 |
Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VSRlCGSSMsALhtaaqaI |
Chain | Residue | Details |
C | VAL91-ILE109 |
site_id | PS00099 |
Number of Residues | 14 |
Details | THIOLASE_3 Thiolases active site. GLSTMCIGlGqGiA |
Chain | Residue | Details |
C | GLY372-ALA385 |
site_id | PS00166 |
Number of Residues | 21 |
Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VAaINGialGGGlemcLaADF |
Chain | Residue | Details |
A | VAL107-PHE127 |
site_id | PS00178 |
Number of Residues | 11 |
Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pk.GGtVTAGTS |
Chain | Residue | Details |
C | PRO232-SER242 |
site_id | PS00737 |
Number of Residues | 17 |
Details | THIOLASE_2 Thiolases signature 2. NlhGGaIAlGHPfGcSG |
Chain | Residue | Details |
C | ASN337-GLY353 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-thioester intermediate => ECO:0000255|HAMAP-Rule:MF_01620 |
Chain | Residue | Details |
C | GLY96 | |
D | GLY96 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01620 |
Chain | Residue | Details |
C | PRO348 | |
B | ASP297 | |
B | MET325 | |
B | ASP344 | |
B | VAL401 | |
B | LYS408 | |
B | SER430 | |
B | ASN454 | |
B | ASN501 | |
B | TYR660 | |
C | ILE378 | |
D | PRO348 | |
D | ILE378 | |
A | LYS408 | |
A | SER430 | |
A | ASN454 | |
A | ASN501 | |
A | TYR660 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01621 |
Chain | Residue | Details |
A | GLU120 | |
A | GLU140 | |
B | GLU120 | |
B | GLU140 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
C | HIS347 | |
C | CYS377 | |
C | CYS95 | |
C | GLY379 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
B | GLU140 | |
B | GLY148 |
site_id | CSA11 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
A | GLU120 | |
A | GLU140 | |
A | GLY117 |
site_id | CSA12 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
B | GLU120 | |
B | GLU140 | |
B | GLY117 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
D | HIS347 | |
D | CYS377 | |
D | CYS95 | |
D | GLY379 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
A | GLU120 | |
A | GLU140 | |
A | GLY117 | |
A | ALA69 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
B | GLU120 | |
B | GLU140 | |
B | GLY117 | |
B | ALA69 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
C | HIS347 | |
C | CYS377 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
D | HIS347 | |
D | CYS377 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
A | HIS451 | |
A | SER430 | |
A | ASN501 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
B | HIS451 | |
B | SER430 | |
B | ASN501 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
A | GLU140 | |
A | GLY148 |