2JI7
X-ray structure of Oxalyl-CoA decarboxylase with covalent reaction intermediate
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 | 51 |
| Details | BINDING SITE FOR RESIDUE OXT B1566 |
| Chain | Residue |
| A | VAL32 |
| B | THR265 |
| B | ARG266 |
| B | ALA267 |
| B | TRP285 |
| B | LEU286 |
| B | ASN358 |
| B | LYS359 |
| B | LEU362 |
| B | TYR377 |
| B | GLY400 |
| A | GLU56 |
| B | ALA401 |
| B | ASN402 |
| B | ALA403 |
| B | LEU404 |
| B | ASP405 |
| B | ARG408 |
| B | MET409 |
| B | GLY426 |
| B | MET428 |
| B | GLY451 |
| A | VAL79 |
| B | ASP452 |
| B | SER453 |
| B | ALA454 |
| B | PHE457 |
| B | ASN479 |
| B | GLY481 |
| B | ILE482 |
| B | TYR483 |
| B | ARG555 |
| B | MG1567 |
| A | ASN86 |
| B | HOH2437 |
| B | HOH2457 |
| B | HOH2483 |
| B | HOH2559 |
| B | HOH2571 |
| B | HOH2572 |
| B | HOH2573 |
| B | HOH2574 |
| B | HOH2575 |
| B | HOH2576 |
| A | TYR120 |
| B | HOH2577 |
| B | HOH2578 |
| A | GLU121 |
| A | HOH2032 |
| B | ALA263 |
| B | ALA264 |
| site_id | AC2 |
| Number of Residues | 53 |
| Details | BINDING SITE FOR RESIDUE OXT A1566 |
| Chain | Residue |
| B | VAL79 |
| B | ASN86 |
| B | TYR120 |
| B | GLU121 |
| B | HOH2039 |
| A | ALA263 |
| A | ALA264 |
| A | THR265 |
| A | ARG266 |
| A | ALA267 |
| A | TRP285 |
| A | LEU286 |
| A | ASN358 |
| A | LYS359 |
| A | LEU362 |
| A | TYR377 |
| A | GLY400 |
| A | ALA401 |
| A | ASN402 |
| A | ALA403 |
| A | LEU404 |
| A | ASP405 |
| A | ARG408 |
| A | MET409 |
| A | GLY426 |
| A | MET428 |
| A | GLY451 |
| A | ASP452 |
| A | SER453 |
| A | ALA454 |
| A | PHE457 |
| A | ASN479 |
| A | GLY481 |
| A | ILE482 |
| A | TYR483 |
| A | ARG555 |
| A | MG1567 |
| A | HOH2435 |
| A | HOH2436 |
| A | HOH2457 |
| A | HOH2479 |
| A | HOH2556 |
| A | HOH2570 |
| A | HOH2571 |
| A | HOH2572 |
| A | HOH2573 |
| A | HOH2574 |
| A | HOH2575 |
| A | HOH2576 |
| A | HOH2577 |
| A | HOH2578 |
| B | VAL32 |
| B | GLU56 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B1567 |
| Chain | Residue |
| B | ASP452 |
| B | ASN479 |
| B | GLY481 |
| B | OXT1566 |
| B | HOH2483 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A1567 |
| Chain | Residue |
| A | ASP452 |
| A | ASN479 |
| A | GLY481 |
| A | OXT1566 |
| A | HOH2479 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP B1568 |
| Chain | Residue |
| B | ARG160 |
| B | GLY221 |
| B | LYS222 |
| B | GLY223 |
| B | TYR226 |
| B | MET247 |
| B | GLY280 |
| B | ARG282 |
| B | LEU286 |
| B | ASP306 |
| B | ILE307 |
| B | GLY324 |
| B | ASP325 |
| B | ILE326 |
| B | HOH2308 |
| B | HOH2579 |
| B | HOH2580 |
| B | HOH2581 |
| B | HOH2583 |
| 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 | ALA281 |
| A | ARG282 |
| A | LEU286 |
| A | ASP306 |
| A | ILE307 |
| A | GLY324 |
| A | ASP325 |
| A | ILE326 |
| A | HOH2266 |
| A | HOH2458 |
| A | HOH2580 |
| A | HOH2581 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE A1569 |
| Chain | Residue |
| A | GLU70 |
| A | ALA193 |
| A | TYR226 |
| A | HOH2270 |
| A | HOH2583 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE B1569 |
| Chain | Residue |
| B | ALA193 |
| B | ALA227 |
| B | GLN228 |
| B | HOH2284 |
| B | HOH2582 |
| B | HOH2583 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE B3P A1570 |
| Chain | Residue |
| A | ASP489 |
| A | GLY493 |
| A | VAL494 |
| A | ARG499 |
| A | HOH2584 |
| B | ASN469 |
| B | LYS537 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE B3P B1570 |
| Chain | Residue |
| A | GLU369 |
| B | MET366 |
| B | THR367 |
| B | GLY382 |
| B | ARG385 |
| B | ASP386 |
| B | HOH2585 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE B3P B1571 |
| Chain | Residue |
| A | ASN469 |
| A | HOH2474 |
| B | ASP489 |
| B | GLY493 |
| B | VAL494 |
| B | ARG499 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE B3P A1571 |
| Chain | Residue |
| A | MET366 |
| A | THR367 |
| A | GLY382 |
| A | VAL383 |
| A | ARG385 |
| A | ASP386 |
| A | HOH2398 |
| A | HOH2417 |
| A | HOH2420 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE B3P B1572 |
| Chain | Residue |
| A | LYS291 |
| B | GLU109 |
| B | GLU111 |
| B | SER141 |
| B | LYS143 |
| B | ASP144 |
| B | HOH2587 |
| B | HOH2589 |
| B | HOH2592 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE B3P A1572 |
| Chain | Residue |
| A | GLU109 |
| A | GLU111 |
| A | LYS143 |
| A | ASP144 |
| A | HOH2588 |
| A | HOH2591 |
| A | HOH2593 |
| B | LYS291 |
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 |
