2GD2
The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006637 | biological_process | acyl-CoA metabolic process |
| A | 0008111 | molecular_function | alpha-methylacyl-CoA racemase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006637 | biological_process | acyl-CoA metabolic process |
| B | 0008111 | molecular_function | alpha-methylacyl-CoA racemase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006637 | biological_process | acyl-CoA metabolic process |
| C | 0008111 | molecular_function | alpha-methylacyl-CoA racemase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006637 | biological_process | acyl-CoA metabolic process |
| D | 0008111 | molecular_function | alpha-methylacyl-CoA racemase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE CAA A 1751 |
| Chain | Residue |
| A | ILE16 |
| A | ARG91 |
| A | LEU92 |
| A | GLY113 |
| A | ALA124 |
| A | GLY125 |
| A | HIS126 |
| A | ASP127 |
| A | TYR130 |
| A | ASP156 |
| A | HOH1801 |
| A | ARG38 |
| A | HOH1826 |
| A | HOH1887 |
| A | HOH1920 |
| A | HOH1992 |
| A | HOH1999 |
| A | HOH2016 |
| A | HOH2048 |
| A | HOH2143 |
| A | ALA59 |
| A | LEU61 |
| A | LYS62 |
| A | GLY83 |
| A | TYR84 |
| A | ARG85 |
| A | VAL88 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CAA B 1752 |
| Chain | Residue |
| B | ILE16 |
| B | ARG38 |
| B | ALA59 |
| B | LEU61 |
| B | LYS62 |
| B | GLY83 |
| B | TYR84 |
| B | ARG85 |
| B | VAL88 |
| B | ARG91 |
| B | LEU92 |
| B | GLY113 |
| B | GLY125 |
| B | TYR130 |
| B | GOL2308 |
| B | HOH2350 |
| B | HOH2388 |
| B | HOH2402 |
| B | HOH2427 |
| B | HOH2451 |
| B | HOH2473 |
| B | HOH2505 |
| B | HOH2567 |
| B | HOH2613 |
| B | HOH2677 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE CAA C 1753 |
| Chain | Residue |
| C | ARG38 |
| C | ALA59 |
| C | ASP60 |
| C | LEU61 |
| C | LYS62 |
| C | GLY83 |
| C | TYR84 |
| C | ARG85 |
| C | VAL88 |
| C | ARG91 |
| C | LEU92 |
| C | GLY113 |
| C | GLY125 |
| C | TYR130 |
| C | ASP156 |
| C | GOL2307 |
| C | HOH2337 |
| C | HOH2367 |
| C | HOH2397 |
| C | HOH2434 |
| C | HOH2478 |
| C | HOH2499 |
| C | HOH2566 |
| C | HOH2642 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE CAA D 1754 |
| Chain | Residue |
| D | HOH1987 |
| D | HOH2031 |
| D | HOH2045 |
| D | HOH2046 |
| D | HOH2083 |
| D | HOH2087 |
| D | HOH2141 |
| D | HOH2152 |
| D | ILE16 |
| D | ARG38 |
| D | ALA59 |
| D | ASP60 |
| D | LEU61 |
| D | LYS62 |
| D | GLY83 |
| D | TYR84 |
| D | ARG85 |
| D | VAL88 |
| D | ARG91 |
| D | LEU92 |
| D | GLY113 |
| D | GLY125 |
| D | HIS126 |
| D | ASP127 |
| D | TYR130 |
| D | ASP156 |
| D | HOH1819 |
| D | HOH1830 |
| D | HOH1836 |
| D | HOH1872 |
| D | HOH1976 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 2307 |
| Chain | Residue |
| C | ILE16 |
| C | HIS126 |
| C | ASP127 |
| C | ASP156 |
| C | CAA1753 |
| C | HOH2561 |
| D | LEU217 |
| D | ILE240 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 2308 |
| Chain | Residue |
| A | TYR224 |
| B | ILE16 |
| B | HIS126 |
| B | ASP127 |
| B | ASP156 |
| B | CAA1752 |
| B | HOH2662 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17320106","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22360758","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17320106","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22360758","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17320106","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22360758","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| A | ASP156 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| B | ASP156 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| C | ASP156 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| D | ASP156 |
