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 | 0008949 | molecular_function | oxalyl-CoA decarboxylase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| 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 | 0008949 | molecular_function | oxalyl-CoA decarboxylase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| 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 | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16216870","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17637344","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
