3MDE
CRYSTAL STRUCTURES OF MEDIUM CHAIN ACYL-COA DEHYDROGENASE FROM PIG LIVER MITOCHONDRIA WITH AND WITHOUT SUBSTRATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001889 | biological_process | liver development |
A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005978 | biological_process | glycogen biosynthetic process |
A | 0006082 | biological_process | organic acid metabolic process |
A | 0006111 | biological_process | regulation of gluconeogenesis |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0007507 | biological_process | heart development |
A | 0009409 | biological_process | response to cold |
A | 0009437 | biological_process | carnitine metabolic process |
A | 0009791 | biological_process | post-embryonic development |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0019254 | biological_process | carnitine metabolic process, CoA-linked |
A | 0030424 | cellular_component | axon |
A | 0031966 | cellular_component | mitochondrial membrane |
A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
A | 0042594 | biological_process | response to starvation |
A | 0042802 | molecular_function | identical protein binding |
A | 0045329 | biological_process | carnitine biosynthetic process |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0051791 | biological_process | medium-chain fatty acid metabolic process |
A | 0051793 | biological_process | medium-chain fatty acid catabolic process |
A | 0055007 | biological_process | cardiac muscle cell differentiation |
A | 0070991 | molecular_function | medium-chain fatty acyl-CoA dehydrogenase activity |
B | 0001889 | biological_process | liver development |
B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005978 | biological_process | glycogen biosynthetic process |
B | 0006082 | biological_process | organic acid metabolic process |
B | 0006111 | biological_process | regulation of gluconeogenesis |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0007507 | biological_process | heart development |
B | 0009409 | biological_process | response to cold |
B | 0009437 | biological_process | carnitine metabolic process |
B | 0009791 | biological_process | post-embryonic development |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0019254 | biological_process | carnitine metabolic process, CoA-linked |
B | 0030424 | cellular_component | axon |
B | 0031966 | cellular_component | mitochondrial membrane |
B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
B | 0042594 | biological_process | response to starvation |
B | 0042802 | molecular_function | identical protein binding |
B | 0045329 | biological_process | carnitine biosynthetic process |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0051791 | biological_process | medium-chain fatty acid metabolic process |
B | 0051793 | biological_process | medium-chain fatty acid catabolic process |
B | 0055007 | biological_process | cardiac muscle cell differentiation |
B | 0070991 | molecular_function | medium-chain fatty acyl-CoA dehydrogenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE CO8 A 400 |
Chain | Residue |
A | THR96 |
A | MET249 |
A | PHE252 |
A | ASP253 |
A | ARG256 |
A | ARG324 |
A | THR326 |
A | TYR375 |
A | GLU376 |
A | GLY377 |
A | ILE381 |
A | GLU99 |
A | FAD399 |
A | HOH803 |
A | HOH845 |
A | HOH860 |
A | HOH868 |
A | HOH888 |
A | HOH986 |
A | LEU103 |
A | GLY141 |
A | SER142 |
A | VAL144 |
A | ALA145 |
A | SER191 |
A | PHE245 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CO8 B 400 |
Chain | Residue |
B | THR96 |
B | GLU99 |
B | LEU103 |
B | GLY141 |
B | SER142 |
B | VAL144 |
B | SER191 |
B | PHE245 |
B | MET249 |
B | PHE252 |
B | THR326 |
B | TYR375 |
B | GLU376 |
B | GLY377 |
B | FAD399 |
B | HOH946 |
B | HOH960 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD A 399 |
Chain | Residue |
A | TYR133 |
A | VAL135 |
A | THR136 |
A | GLY141 |
A | SER142 |
A | TRP166 |
A | ILE167 |
A | THR168 |
A | ILE371 |
A | ILE374 |
A | THR378 |
A | GLN380 |
A | CO8400 |
A | HOH802 |
A | HOH804 |
A | HOH805 |
A | HOH846 |
A | HOH850 |
B | ARG281 |
B | THR283 |
B | PHE284 |
B | LEU288 |
B | GLN292 |
B | ILE294 |
B | GLN349 |
B | VAL350 |
B | GLY353 |
B | HOH806 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD B 399 |
Chain | Residue |
A | ARG281 |
A | THR283 |
A | PHE284 |
A | LEU288 |
A | HIS291 |
A | GLN292 |
A | GLN349 |
A | VAL350 |
A | GLY353 |
B | TYR133 |
B | VAL135 |
B | THR136 |
B | GLY141 |
B | SER142 |
B | TRP166 |
B | THR168 |
B | ILE371 |
B | ILE374 |
B | TYR375 |
B | THR378 |
B | GLN380 |
B | CO8400 |
B | HOH901 |
B | HOH903 |
B | HOH904 |
B | HOH925 |
B | HOH926 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:12966080, ECO:0000269|PubMed:8356049 |
Chain | Residue | Details |
A | GLU376 | |
B | GLU376 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: in other chain => ECO:0000269|PubMed:12966080, ECO:0000269|PubMed:8356049, ECO:0007744|PDB:1UDY, ECO:0007744|PDB:3MDD, ECO:0007744|PDB:3MDE |
Chain | Residue | Details |
A | TYR133 | |
A | TRP166 | |
A | HIS291 | |
A | GLY377 | |
B | TYR133 | |
B | TRP166 | |
B | HIS291 | |
B | GLY377 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8356049, ECO:0007744|PDB:3MDE |
Chain | Residue | Details |
A | SER142 | |
B | ASP253 | |
B | ARG256 | |
B | ARG324 | |
B | THR326 | |
B | GLU376 | |
A | SER191 | |
A | ASP253 | |
A | ARG256 | |
A | ARG324 | |
A | THR326 | |
A | GLU376 | |
B | SER142 | |
B | SER191 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12966080, ECO:0000269|PubMed:8356049, ECO:0007744|PDB:1UDY, ECO:0007744|PDB:3MDD, ECO:0007744|PDB:3MDE |
Chain | Residue | Details |
A | ARG281 | |
B | ARG281 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8356049 |
Chain | Residue | Details |
A | GLN349 | |
B | GLN349 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P45952 |
Chain | Residue | Details |
A | LYS54 | |
B | LYS54 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P45952 |
Chain | Residue | Details |
A | LYS154 | |
B | LYS154 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 |
Chain | Residue | Details |
A | LYS187 | |
A | LYS192 | |
A | LYS234 | |
A | LYS246 | |
B | LYS187 | |
B | LYS192 | |
B | LYS234 | |
B | LYS246 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P11310 |
Chain | Residue | Details |
A | LYS254 | |
A | LYS276 | |
B | LYS254 | |
B | LYS276 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P45952 |
Chain | Residue | Details |
A | THR326 | |
B | THR326 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | THR255 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | THR255 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | GLU376 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | GLU376 |
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 893 |
Chain | Residue | Details |
A | GLU376 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 1 |
Details | M-CSA 893 |
Chain | Residue | Details |
B | GLU376 | proton shuttle (general acid/base) |