2JI6
X-ray structure of Oxalyl-CoA decarboxylase in complex with 3-deaza- ThDP and oxalyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0003824 | molecular_function | catalytic activity |
| 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 | 37 |
| Details | BINDING SITE FOR RESIDUE OXK A1569 |
| Chain | Residue |
| A | ALA263 |
| A | LEU362 |
| A | GLY400 |
| A | LEU404 |
| A | ASP405 |
| A | ARG408 |
| A | MET409 |
| A | GLY426 |
| A | MET428 |
| A | TYR483 |
| A | SER553 |
| A | ALA264 |
| A | ARG555 |
| A | ILE556 |
| A | TPW1566 |
| A | HOH2209 |
| A | HOH2336 |
| A | HOH2452 |
| A | HOH2453 |
| A | HOH2454 |
| A | HOH2455 |
| A | HOH2456 |
| A | THR265 |
| A | HOH2457 |
| A | HOH2458 |
| A | HOH2459 |
| A | HOH2460 |
| B | GLY33 |
| B | ILE34 |
| B | TYR120 |
| B | HOH2112 |
| A | ARG266 |
| A | ALA267 |
| A | TRP285 |
| A | LEU286 |
| A | ASN358 |
| A | LYS359 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE OXK B1569 |
| Chain | Residue |
| A | GLY33 |
| A | ILE34 |
| A | TYR120 |
| A | HOH2085 |
| B | ALA263 |
| B | ALA264 |
| 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 | MET428 |
| B | TYR483 |
| B | SER553 |
| B | ARG555 |
| B | ILE556 |
| B | TPW1566 |
| B | HOH2327 |
| B | HOH2435 |
| B | HOH2436 |
| B | HOH2437 |
| B | HOH2438 |
| B | HOH2439 |
| B | HOH2440 |
| B | HOH2441 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPW B1566 |
| Chain | Residue |
| A | VAL32 |
| A | GLU56 |
| A | ASN86 |
| A | GLU121 |
| B | TYR377 |
| B | GLY400 |
| B | ALA401 |
| B | ASN402 |
| B | ALA403 |
| B | GLY426 |
| B | MET428 |
| B | GLY451 |
| B | ASP452 |
| B | SER453 |
| B | ALA454 |
| B | PHE457 |
| B | ASN479 |
| B | GLY481 |
| B | ILE482 |
| B | TYR483 |
| B | MG1567 |
| B | OXK1569 |
| B | HOH2433 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPW A1566 |
| Chain | Residue |
| A | MET428 |
| A | GLY451 |
| A | ASP452 |
| A | SER453 |
| A | ALA454 |
| A | PHE457 |
| A | ASN479 |
| A | GLY481 |
| A | ILE482 |
| A | TYR483 |
| A | MG1567 |
| A | OXK1569 |
| A | HOH2374 |
| B | VAL32 |
| B | GLU56 |
| B | VAL79 |
| B | GLY83 |
| B | ASN86 |
| B | GLU121 |
| A | TYR377 |
| A | GLY400 |
| A | ALA401 |
| A | ASN402 |
| A | ALA403 |
| A | GLY426 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B1567 |
| Chain | Residue |
| B | ASP452 |
| B | ASN479 |
| B | GLY481 |
| B | TPW1566 |
| B | HOH2433 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A1567 |
| Chain | Residue |
| A | ASP452 |
| A | ASN479 |
| A | GLY481 |
| A | TPW1566 |
| A | HOH2374 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP B1568 |
| Chain | Residue |
| B | ARG160 |
| B | GLY221 |
| B | LYS222 |
| B | GLY223 |
| B | MET247 |
| B | GLY280 |
| B | ALA281 |
| B | ARG282 |
| B | ASP306 |
| B | ILE307 |
| B | GLY324 |
| B | ASP325 |
| B | ILE326 |
| B | PGE1570 |
| B | HOH2208 |
| B | HOH2239 |
| B | HOH2344 |
| B | HOH2434 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP A1568 |
| Chain | Residue |
| A | ARG160 |
| A | GLY221 |
| A | LYS222 |
| A | GLY223 |
| A | MET247 |
| A | GLY280 |
| A | ALA281 |
| A | ARG282 |
| A | LEU286 |
| A | ASP306 |
| A | ILE307 |
| A | GLY324 |
| A | ASP325 |
| A | ILE326 |
| A | HOH2350 |
| A | HOH2449 |
| A | HOH2450 |
| A | HOH2451 |
| A | HOH2461 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PGE A1570 |
| Chain | Residue |
| A | GLU70 |
| A | ALA193 |
| A | PRO194 |
| A | TYR226 |
| A | ALA227 |
| A | ASP325 |
| A | HOH2191 |
| A | HOH2461 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE B1570 |
| Chain | Residue |
| B | ALA193 |
| B | PRO194 |
| B | TYR226 |
| B | ALA227 |
| B | ADP1568 |
| B | HOH2209 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE B3P A1571 |
| Chain | Residue |
| A | ASP489 |
| A | GLY493 |
| A | VAL494 |
| A | ARG499 |
| A | HOH2386 |
| A | HOH2462 |
| A | HOH2464 |
| B | ASN469 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE B3P B1571 |
| Chain | Residue |
| A | ASN469 |
| A | LYS537 |
| A | HOH2368 |
| B | ASP489 |
| B | GLY493 |
| B | VAL494 |
| B | ARG499 |
| B | HOH2444 |
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 |
