1X7W
Crystal structure of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0009083 | biological_process | branched-chain amino acid catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
A | 0046872 | molecular_function | metal ion binding |
A | 0047101 | molecular_function | branched-chain alpha-keto acid dehydrogenase activity |
A | 0160157 | cellular_component | branched-chain alpha-ketoacid dehydrogenase complex |
B | 0003824 | molecular_function | catalytic activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 701 |
Chain | Residue |
A | GLN112 |
A | SER161 |
A | PRO163 |
A | THR166 |
A | GLN167 |
A | HOH807 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K B 702 |
Chain | Residue |
B | CYS178 |
B | ASP181 |
B | ASN183 |
B | HOH920 |
B | GLY128 |
B | LEU130 |
B | THR131 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 703 |
Chain | Residue |
A | GLU193 |
A | ASN222 |
A | TYR224 |
A | TPP801 |
A | HOH812 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 704 |
Chain | Residue |
A | TYR113 |
A | TPP801 |
B | TYR102 |
B | HIS146 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE TPP A 801 |
Chain | Residue |
A | ARG114 |
A | SER162 |
A | LEU164 |
A | GLY192 |
A | GLU193 |
A | GLY194 |
A | ALA195 |
A | GLU198 |
A | ARG220 |
A | ASN222 |
A | TYR224 |
A | ALA225 |
A | ILE226 |
A | MN703 |
A | CL704 |
A | HOH812 |
A | HOH846 |
A | HOH869 |
A | HOH873 |
B | GLU46 |
B | LEU74 |
B | GLU76 |
B | GLN98 |
B | TYR102 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 901 |
Chain | Residue |
A | GLN374 |
B | TRP260 |
B | THR284 |
B | GLU290 |
B | THR294 |
B | ARG309 |
B | HOH954 |
B | HOH1163 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW |
Chain | Residue | Details |
B | TYR102 | |
A | ALA195 | |
A | ARG220 | |
A | ASN222 | |
A | TYR224 | |
A | HIS291 | |
B | GLY128 | |
B | LEU130 | |
B | THR131 | |
B | CYS178 | |
B | ASP181 | |
B | ASN183 | |
A | GLU193 | |
A | GLY194 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q6P3A8 |
Chain | Residue | Details |
B | LYS182 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
B | LYS191 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P50136 |
Chain | Residue | Details |
A | SER294 | |
A | SER302 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P50136 |
Chain | Residue | Details |
A | LYS311 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P50136 |
Chain | Residue | Details |
A | LYS335 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dtw |
Chain | Residue | Details |
B | GLU76 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dtw |
Chain | Residue | Details |
B | GLU76 | |
B | HIS146 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 280 |
Chain | Residue | Details |
A | GLU76 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
A | SER162 | hydrogen bond acceptor, steric role |
A | HIS291 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLN292 | hydrogen bond acceptor, hydrogen bond donor |