1RX0
Crystal structure of isobutyryl-CoA dehydrogenase complexed with substrate/ligand.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006574 | biological_process | valine catabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0009083 | biological_process | branched-chain amino acid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0102035 | molecular_function | 2-methylpropanoyl-CoA dehydrogenase activity |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006574 | biological_process | valine catabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0009083 | biological_process | branched-chain amino acid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0102035 | molecular_function | 2-methylpropanoyl-CoA dehydrogenase activity |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0006574 | biological_process | valine catabolic process |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0009083 | biological_process | branched-chain amino acid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0102035 | molecular_function | 2-methylpropanoyl-CoA dehydrogenase activity |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0006574 | biological_process | valine catabolic process |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0009083 | biological_process | branched-chain amino acid catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0102035 | molecular_function | 2-methylpropanoyl-CoA dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 2001 |
| Chain | Residue |
| A | HOH9289 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 2002 |
| Chain | Residue |
| C | PHE31 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 2003 |
| Chain | Residue |
| B | PHE169 |
| B | GLU211 |
| B | HOH9370 |
| D | TYR354 |
| D | LEU357 |
| D | HOH9255 |
| D | HOH9339 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 2004 |
| Chain | Residue |
| B | ILE193 |
| B | PHE244 |
| B | ALA247 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 2005 |
| Chain | Residue |
| C | ARG249 |
| C | GLU321 |
| C | ARG322 |
| C | HOH9149 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 2006 |
| Chain | Residue |
| B | PRO15 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 2007 |
| Chain | Residue |
| B | HIS276 |
| B | TYR360 |
| B | HOH9021 |
| B | HOH9391 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 2008 |
| Chain | Residue |
| A | PRO141 |
| C | TYR354 |
| C | TYR360 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO D 2009 |
| Chain | Residue |
| D | THR92 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 2010 |
| Chain | Residue |
| B | HOH9319 |
| D | PHE283 |
| D | GLY284 |
| D | HOH9254 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 2011 |
| Chain | Residue |
| A | LYS156 |
| A | ARG236 |
| A | HOH9009 |
| site_id | BC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD A 399 |
| Chain | Residue |
| A | TYR136 |
| A | LEU138 |
| A | THR139 |
| A | GLY144 |
| A | SER145 |
| A | PHE169 |
| A | ILE170 |
| A | SER171 |
| A | TRP216 |
| A | VAL371 |
| A | LEU375 |
| A | SER378 |
| A | GLU380 |
| A | HOH9118 |
| A | HOH9123 |
| A | HOH9209 |
| A | HOH9210 |
| B | GLN291 |
| C | ARG280 |
| C | PHE283 |
| C | ASN290 |
| C | LEU293 |
| C | GLN349 |
| C | MET350 |
| C | GLY353 |
| C | TYR354 |
| C | HOH9082 |
| C | HOH9083 |
| site_id | BC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD B 399 |
| Chain | Residue |
| A | GLN291 |
| B | TYR136 |
| B | LEU138 |
| B | THR139 |
| B | GLY144 |
| B | SER145 |
| B | PHE169 |
| B | ILE170 |
| B | SER171 |
| B | TRP216 |
| B | VAL371 |
| B | LEU375 |
| B | SER378 |
| B | GLU380 |
| B | HOH9326 |
| B | HOH9381 |
| B | HOH9402 |
| D | ARG280 |
| D | PHE283 |
| D | ASN290 |
| D | LEU293 |
| D | GLN349 |
| D | MET350 |
| D | GLY352 |
| D | GLY353 |
| D | TYR354 |
| D | ACY9002 |
| D | HOH9273 |
| D | HOH9274 |
| site_id | BC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD C 399 |
| Chain | Residue |
| C | TYR136 |
| C | LEU138 |
| C | THR139 |
| C | GLY144 |
| C | SER145 |
| C | PHE169 |
| C | ILE170 |
| C | SER171 |
| C | VAL371 |
| C | LEU375 |
| C | SER378 |
| C | GLU380 |
| C | 2MC400 |
| C | HOH9137 |
| C | HOH9270 |
| C | HOH9271 |
| C | HOH9329 |
| D | GLN291 |
| A | ARG280 |
| A | PHE283 |
| A | ASN290 |
| A | LEU293 |
| A | GLN349 |
| A | MET350 |
| A | GLY352 |
| A | GLY353 |
| A | TYR354 |
| A | HOH9361 |
| site_id | BC6 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD D 399 |
| Chain | Residue |
| B | ARG280 |
| B | PHE283 |
| B | ASN290 |
| B | LEU293 |
| B | GLN349 |
| B | MET350 |
| B | GLY352 |
| B | GLY353 |
| B | TYR354 |
| B | ACY9001 |
| B | HOH9390 |
| C | GLN291 |
| D | TYR136 |
| D | LEU138 |
| D | THR139 |
| D | GLY144 |
| D | SER145 |
| D | PHE169 |
| D | ILE170 |
| D | SER171 |
| D | VAL371 |
| D | ILE374 |
| D | LEU375 |
| D | SER378 |
| D | GLU380 |
| D | 2MC400 |
| D | HOH9334 |
| D | HOH9346 |
| D | HOH9347 |
| site_id | BC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 2MC C 400 |
| Chain | Residue |
| C | ILE103 |
| C | TYR136 |
| C | THR139 |
| C | SER145 |
| C | ALA147 |
| C | PHE244 |
| C | VAL248 |
| C | LEU251 |
| C | ASN252 |
| C | ARG255 |
| C | VAL326 |
| C | LEU375 |
| C | GLU376 |
| C | GLY377 |
| C | LEU385 |
| C | ARG388 |
| C | FAD399 |
| C | HOH9202 |
| C | HOH9203 |
| C | HOH9269 |
| C | HOH9349 |
| C | HOH9350 |
| site_id | BC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 2MC D 400 |
| Chain | Residue |
| D | ILE103 |
| D | TYR136 |
| D | THR139 |
| D | SER145 |
| D | ALA147 |
| D | PHE244 |
| D | VAL248 |
| D | LEU251 |
| D | ASN252 |
| D | ARG255 |
| D | VAL326 |
| D | LEU375 |
| D | GLU376 |
| D | GLY377 |
| D | LEU385 |
| D | ARG388 |
| D | FAD399 |
| D | HOH9128 |
| D | HOH9129 |
| D | HOH9130 |
| D | HOH9333 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY B 9001 |
| Chain | Residue |
| B | HOH9141 |
| D | FAD399 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACY D 9002 |
| Chain | Residue |
| B | FAD399 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY D 9003 |
| Chain | Residue |
| D | LEU62 |
| D | PHE64 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY C 9004 |
| Chain | Residue |
| C | GLY142 |
| C | SER143 |
| C | SER149 |
| C | HOH9267 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY A 9005 |
| Chain | Residue |
| A | TYR68 |
| A | LEU78 |
| A | ARG80 |
| A | TRP109 |
| A | HOH9088 |
| A | HOH9089 |
| A | HOH9090 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY B 9006 |
| Chain | Residue |
| B | GLN61 |
| B | LEU62 |
| B | GLY63 |
| B | HOH9118 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY D 9007 |
| Chain | Residue |
| D | ARG312 |
| D | HOH9312 |
Functional Information from PROSITE/UniProt
| site_id | PS00072 |
| Number of Residues | 13 |
| Details | ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CLTEpgSGSDaaS |
| Chain | Residue | Details |
| A | CYS137-SER149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:14752098 |
| Chain | Residue | Details |
| A | GLU376 | |
| B | GLU376 | |
| C | GLU376 | |
| D | GLU376 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:14752098 |
| Chain | Residue | Details |
| A | TYR136 | |
| D | TYR136 | |
| D | PHE169 | |
| D | SER378 | |
| A | PHE169 | |
| A | SER378 | |
| B | TYR136 | |
| B | PHE169 | |
| B | SER378 | |
| C | TYR136 | |
| C | PHE169 | |
| C | SER378 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14752098 |
| Chain | Residue | Details |
| A | SER145 | |
| B | ASN290 | |
| B | GLN349 | |
| B | ARG388 | |
| C | SER145 | |
| C | ASN252 | |
| C | ARG280 | |
| C | ASN290 | |
| C | GLN349 | |
| C | ARG388 | |
| D | SER145 | |
| A | ASN252 | |
| D | ASN252 | |
| D | ARG280 | |
| D | ASN290 | |
| D | GLN349 | |
| D | ARG388 | |
| A | ARG280 | |
| A | ASN290 | |
| A | GLN349 | |
| A | ARG388 | |
| B | SER145 | |
| B | ASN252 | |
| B | ARG280 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9D7B6 |
| Chain | Residue | Details |
| A | LYS28 | |
| B | LYS28 | |
| C | LYS28 | |
| D | LYS28 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D7B6 |
| Chain | Residue | Details |
| A | LYS191 | |
| B | LYS191 | |
| C | LYS191 | |
| D | LYS191 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D7B6 |
| Chain | Residue | Details |
| A | LYS209 | |
| B | LYS209 | |
| C | LYS209 | |
| D | LYS209 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLY254 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLY254 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | GLY254 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | GLY254 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLU376 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLU376 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | GLU376 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | GLU376 |
