2JI8
X-ray structure of Oxalyl-CoA decarboxylase in complex with Formyl- CoA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0001561 | biological_process | fatty acid alpha-oxidation |
A | 0003824 | molecular_function | catalytic activity |
A | 0005777 | cellular_component | peroxisome |
A | 0008949 | molecular_function | oxalyl-CoA decarboxylase activity |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0033611 | biological_process | oxalate catabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0043531 | molecular_function | ADP binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0001561 | biological_process | fatty acid alpha-oxidation |
B | 0003824 | molecular_function | catalytic activity |
B | 0005777 | cellular_component | peroxisome |
B | 0008949 | molecular_function | oxalyl-CoA decarboxylase activity |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0033611 | biological_process | oxalate catabolic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0043531 | molecular_function | ADP binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE TPP B1563 |
Chain | Residue |
A | VAL32 |
B | GLY426 |
B | MET428 |
B | GLY451 |
B | ASP452 |
B | SER453 |
B | ALA454 |
B | PHE457 |
B | ASN479 |
B | GLY481 |
B | ILE482 |
A | GLU56 |
B | TYR483 |
B | MG1564 |
B | FYN1566 |
B | HOH2261 |
A | ASN86 |
A | GLU121 |
B | TYR377 |
B | GLY400 |
B | ALA401 |
B | ASN402 |
B | ALA403 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE TPP A1566 |
Chain | Residue |
A | TYR377 |
A | GLY400 |
A | ALA401 |
A | ASN402 |
A | ALA403 |
A | GLY426 |
A | MET428 |
A | GLY451 |
A | ASP452 |
A | SER453 |
A | ALA454 |
A | PHE457 |
A | ASN479 |
A | GLY481 |
A | ILE482 |
A | TYR483 |
A | MG1567 |
A | FYN1569 |
A | HOH2257 |
B | VAL32 |
B | GLU56 |
B | VAL79 |
B | GLY83 |
B | ASN86 |
B | GLU121 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B1564 |
Chain | Residue |
B | ASP452 |
B | ASN479 |
B | GLY481 |
B | TPP1563 |
B | HOH2261 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A1567 |
Chain | Residue |
A | ASP452 |
A | ASN479 |
A | GLY481 |
A | TPP1566 |
A | HOH2257 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ADP B1565 |
Chain | Residue |
B | ARG160 |
B | GLY221 |
B | LYS222 |
B | GLY223 |
B | TYR226 |
B | MET247 |
B | GLY280 |
B | ALA281 |
B | ARG282 |
B | LEU286 |
B | ASP306 |
B | ILE307 |
B | GLY324 |
B | ASP325 |
B | ILE326 |
B | PGE1567 |
B | HOH2173 |
B | HOH2184 |
B | HOH2245 |
B | HOH2293 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP A1568 |
Chain | Residue |
A | ARG160 |
A | GLY221 |
A | LYS222 |
A | GLY223 |
A | TYR226 |
A | MET247 |
A | GLY280 |
A | ARG282 |
A | LEU286 |
A | ASP306 |
A | ILE307 |
A | GLY324 |
A | ASP325 |
A | ILE326 |
A | HOH2145 |
A | HOH2179 |
A | HOH2249 |
A | HOH2305 |
A | HOH2306 |
site_id | AC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FYN B1566 |
Chain | Residue |
B | THR265 |
B | ARG266 |
B | ALA267 |
B | TRP285 |
B | LEU286 |
B | ASN358 |
B | LEU362 |
B | GLY400 |
B | LEU404 |
B | ASP405 |
B | ARG408 |
B | MET409 |
B | GLY426 |
B | TYR483 |
B | SER553 |
B | ARG555 |
B | ILE556 |
B | TPP1563 |
B | HOH2295 |
B | HOH2296 |
B | HOH2297 |
B | ALA263 |
B | ALA264 |
site_id | AC8 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FYN A1569 |
Chain | Residue |
A | ALA263 |
A | ALA264 |
A | THR265 |
A | ARG266 |
A | ALA267 |
A | TRP285 |
A | LEU286 |
A | ASN358 |
A | LYS359 |
A | LEU362 |
A | GLY400 |
A | LEU404 |
A | ARG408 |
A | MET409 |
A | GLY426 |
A | TYR483 |
A | SER553 |
A | ARG555 |
A | ILE556 |
A | TPP1566 |
A | HOH2307 |
A | HOH2308 |
A | HOH2309 |
A | HOH2310 |
A | HOH2311 |
A | HOH2312 |
A | HOH2313 |
A | HOH2314 |
B | TYR120 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PGE A1570 |
Chain | Residue |
A | GLU70 |
A | ALA193 |
A | TYR226 |
A | GLN228 |
A | HOH2306 |
A | HOH2315 |
A | HOH2316 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PGE B1567 |
Chain | Residue |
B | GLU70 |
B | GLY71 |
B | PRO194 |
B | TYR226 |
B | ALA227 |
B | ASP325 |
B | ADP1565 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ILE34 | |
B | TYR120 | |
B | ALA263 | |
B | ALA401 | |
B | ARG408 | |
B | GLY426 | |
B | SER453 | |
B | SER553 | |
A | TYR120 | |
A | ALA263 | |
A | ALA401 | |
A | ARG408 | |
A | GLY426 | |
A | SER453 | |
A | SER553 | |
B | ILE34 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16216870, ECO:0000269|PubMed:17637344 |
Chain | Residue | Details |
A | ARG160 | |
A | TYR483 | |
B | ARG160 | |
B | LYS222 | |
B | ARG282 | |
B | ASP306 | |
B | ILE326 | |
B | TYR377 | |
B | ASP452 | |
B | ASN479 | |
B | GLY481 | |
A | LYS222 | |
B | TYR483 | |
A | ARG282 | |
A | ASP306 | |
A | ILE326 | |
A | TYR377 | |
A | ASP452 | |
A | ASN479 | |
A | GLY481 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASN358 | |
B | ASN358 |