3EXI
Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex with the subunit-binding domain (SBD) of E2p, but SBD cannot be modeled into the electron density
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004738 | molecular_function | pyruvate dehydrogenase activity |
| A | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006086 | biological_process | acetyl-CoA biosynthetic process from pyruvate |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| 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 | 0034604 | molecular_function | pyruvate dehydrogenase (NAD+) activity |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0045254 | cellular_component | pyruvate dehydrogenase complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1902494 | cellular_component | catalytic complex |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006086 | biological_process | acetyl-CoA biosynthetic process from pyruvate |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0034604 | molecular_function | pyruvate dehydrogenase (NAD+) activity |
| B | 0045254 | cellular_component | pyruvate dehydrogenase complex |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1001 |
| Chain | Residue |
| B | ALA160 |
| B | ILE161 |
| B | ASP163 |
| B | HOH2023 |
| B | HOH2034 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1002 |
| Chain | Residue |
| B | HOH2166 |
| A | HOH2050 |
| A | HOH2201 |
| B | GLU173 |
| B | HOH2103 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1003 |
| Chain | Residue |
| A | ARG44 |
| A | ARG314 |
| A | ILE317 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12651851 |
| Chain | Residue | Details |
| B | GLU59 | |
| A | ALA128 | |
| A | TYR198 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12651851, ECO:0000269|PubMed:17474719, ECO:0007744|PDB:1NI4, ECO:0007744|PDB:2OZL |
| Chain | Residue | Details |
| B | ILE112 | |
| A | ARG90 | |
| A | GLY136 | |
| A | VAL138 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12651851, ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061, ECO:0007744|PDB:1NI4, ECO:0007744|PDB:2OZL, ECO:0007744|PDB:3EXE, ECO:0007744|PDB:3EXF, ECO:0007744|PDB:3EXG, ECO:0007744|PDB:3EXH, ECO:0007744|PDB:3EXI |
| Chain | Residue | Details |
| B | ALA160 | |
| B | ASP163 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19081061, ECO:0007744|PDB:3EXE, ECO:0007744|PDB:3EXF, ECO:0007744|PDB:3EXG, ECO:0007744|PDB:3EXH, ECO:0007744|PDB:3EXI |
| Chain | Residue | Details |
| B | ILE161 | |
| A | ALA169 | |
| A | ASN196 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12651851, ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061, ECO:0007744|PDB:1NI4, ECO:0007744|PDB:2OZL, ECO:0007744|PDB:3EXE |
| Chain | Residue | Details |
| B | ASN165 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Important for interaction with DLAT => ECO:0000269|PubMed:20160912 |
| Chain | Residue | Details |
| B | ASP289 | |
| A | LYS215 | |
| A | LYS284 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9D051 |
| Chain | Residue | Details |
| B | TYR37 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D051 |
| Chain | Residue | Details |
| B | LYS324 | |
| A | LYS356 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 => ECO:0000269|PubMed:11486000, ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061 |
| Chain | Residue | Details |
| A | SER264 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P35486 |
| Chain | Residue | Details |
| A | SER266 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 => ECO:0000269|PubMed:11486000, ECO:0000269|PubMed:19081061 |
| Chain | Residue | Details |
| A | SER271 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P35486 |
| Chain | Residue | Details |
| A | TYR272 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS292 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P35486 |
| Chain | Residue | Details |
| A | LYS307 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | GLU59 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | GLU59 | |
| B | HIS128 |
