2GD0
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 | 29 |
Details | BINDING SITE FOR RESIDUE MRS A 1751 |
Chain | Residue |
A | ILE16 |
A | VAL88 |
A | ARG91 |
A | LEU92 |
A | GLY113 |
A | GLY125 |
A | HIS126 |
A | ASP127 |
A | TYR130 |
A | ASP156 |
A | HOH2317 |
A | ASP48 |
A | HOH2356 |
A | HOH2363 |
A | HOH2424 |
A | HOH2639 |
A | HOH2642 |
B | ALA201 |
B | MET202 |
B | THR205 |
B | MET207 |
B | HOH2431 |
A | ALA59 |
A | ASP60 |
A | LEU61 |
A | LYS62 |
A | GLY83 |
A | TYR84 |
A | ARG85 |
site_id | AC2 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE MRS B 1752 |
Chain | Residue |
A | MET202 |
A | THR205 |
A | MET207 |
B | ALA59 |
B | ASP60 |
B | LEU61 |
B | LYS62 |
B | GLY83 |
B | TYR84 |
B | ARG85 |
B | VAL88 |
B | ARG91 |
B | LEU92 |
B | GLY113 |
B | GLY125 |
B | HIS126 |
B | ASP127 |
B | TYR130 |
B | ASN152 |
B | ASP156 |
B | ALA266 |
B | HOH2351 |
B | HOH2360 |
B | HOH2454 |
B | HOH2486 |
B | HOH2517 |
B | HOH2575 |
B | HOH2586 |
B | HOH2594 |
B | HOH2623 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE MRS C 1753 |
Chain | Residue |
C | ASP48 |
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 | HIS126 |
C | ASP127 |
C | TYR130 |
C | ASP156 |
C | HOH2315 |
C | HOH2363 |
C | HOH2364 |
C | HOH2405 |
C | HOH2499 |
C | HOH2655 |
D | THR205 |
D | MET207 |
D | LEU217 |
site_id | AC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE MRS D 1754 |
Chain | Residue |
D | LEU92 |
D | GLY113 |
D | GLY125 |
D | HIS126 |
D | ASP127 |
D | TYR130 |
D | ASN152 |
D | ASP156 |
D | HOH2363 |
D | HOH2367 |
D | HOH2503 |
D | HOH2557 |
D | HOH2565 |
D | HOH2590 |
D | HOH2626 |
C | ALA201 |
C | MET202 |
C | THR205 |
C | MET207 |
D | ILE16 |
D | ALA59 |
D | ASP60 |
D | LEU61 |
D | LYS62 |
D | GLY83 |
D | TYR84 |
D | ARG85 |
D | VAL88 |
D | ARG91 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL C 2302 |
Chain | Residue |
C | MET216 |
C | TYR223 |
C | ILE240 |
C | GLN262 |
C | ASN263 |
C | HOH2389 |
D | PRO261 |
D | ASN263 |
D | ASP264 |
D | HOH2355 |
D | HOH2606 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL D 2303 |
Chain | Residue |
C | PRO261 |
C | ASN263 |
C | HOH2322 |
D | MET216 |
D | ILE240 |
D | GLN262 |
D | ASN263 |
D | HOH2389 |
D | HOH2573 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 2304 |
Chain | Residue |
A | ASN263 |
A | ASP264 |
B | MET216 |
B | TYR223 |
B | ILE240 |
B | GLN262 |
B | ASN263 |
B | HOH2394 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 2306 |
Chain | Residue |
A | MET216 |
A | TYR223 |
A | ILE240 |
A | ASN263 |
A | HOH2392 |
A | HOH2595 |
B | PRO261 |
B | ASN263 |
B | ASP264 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17320106, ECO:0000305|PubMed:22360758 |
Chain | Residue | Details |
A | HIS126 | |
B | HIS126 | |
C | HIS126 | |
D | HIS126 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:17320106, ECO:0000305|PubMed:22360758 |
Chain | Residue | Details |
A | ASP156 | |
B | ASP156 | |
C | ASP156 | |
D | ASP156 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17320106, ECO:0000269|PubMed:22360758 |
Chain | Residue | Details |
A | ARG38 | |
B | GLY125 | |
C | ARG38 | |
C | ALA59 | |
C | GLY83 | |
C | ARG91 | |
C | GLY125 | |
D | ARG38 | |
D | ALA59 | |
D | GLY83 | |
D | ARG91 | |
A | ALA59 | |
D | GLY125 | |
A | GLY83 | |
A | ARG91 | |
A | GLY125 | |
B | ARG38 | |
B | ALA59 | |
B | GLY83 | |
B | ARG91 |
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 |