3N6R
CRYSTAL STRUCTURE OF the holoenzyme of PROPIONYL-COA CARBOXYLASE (PCC)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016874 | molecular_function | ligase activity |
| C | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| D | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| D | 0015977 | biological_process | carbon fixation |
| D | 0016874 | molecular_function | ligase activity |
| E | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| F | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| F | 0015977 | biological_process | carbon fixation |
| F | 0016874 | molecular_function | ligase activity |
| G | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| H | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| H | 0015977 | biological_process | carbon fixation |
| H | 0016874 | molecular_function | ligase activity |
| I | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| I | 0005515 | molecular_function | protein binding |
| I | 0005524 | molecular_function | ATP binding |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| J | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| J | 0005515 | molecular_function | protein binding |
| J | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| J | 0015977 | biological_process | carbon fixation |
| J | 0016874 | molecular_function | ligase activity |
| K | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| K | 0005515 | molecular_function | protein binding |
| K | 0005524 | molecular_function | ATP binding |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| L | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| L | 0005515 | molecular_function | protein binding |
| L | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| L | 0015977 | biological_process | carbon fixation |
| L | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BTI A 801 |
| Chain | Residue |
| A | MET693 |
| A | LYS694 |
| B | PHE397 |
| B | PRO399 |
| J | VAL234 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BTI C 801 |
| Chain | Residue |
| L | THR226 |
| L | VAL234 |
| C | LYS694 |
| D | CYS365 |
| D | GLY396 |
| D | PHE397 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BTI E 801 |
| Chain | Residue |
| E | MET693 |
| E | LYS694 |
| F | CYS365 |
| F | PHE397 |
| F | PRO399 |
| H | THR226 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BTI G 801 |
| Chain | Residue |
| F | VAL234 |
| G | LYS694 |
| H | CYS365 |
| H | GLY396 |
| H | PHE397 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BTI I 801 |
| Chain | Residue |
| B | VAL234 |
| I | MET693 |
| I | LYS694 |
| J | CYS365 |
| J | GLY396 |
| J | PHE397 |
| J | PRO399 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BTI K 801 |
| Chain | Residue |
| D | VAL234 |
| K | MET693 |
| K | LYS694 |
| L | CYS365 |
| L | GLY396 |
| L | PHE397 |
Functional Information from PROSITE/UniProt
| site_id | PS00188 |
| Number of Residues | 18 |
| Details | BIOTIN Biotin-requiring enzymes attachment site. GQaLctIeAMKMeniLrA |
| Chain | Residue | Details |
| A | GLY684-ALA701 |
| site_id | PS00866 |
| Number of Residues | 15 |
| Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASaggGGkG |
| Chain | Residue | Details |
| A | TYR214-GLY228 |
| site_id | PS00867 |
| Number of Residues | 8 |
| Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLEMNTRL |
| Chain | Residue | Details |
| A | PHE347-LEU354 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 474 |
| Details | Domain: {"description":"Biotinyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20725044","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3N6R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20725044","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3N6R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1458 |
| Details | Domain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 198 |
| Details | Region: {"description":"Acyl-CoA binding","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
