2C31
CRYSTAL STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH THE COFACTOR DERIVATIVE THIAMIN-2-THIAZOLONE DIPHOSPHATE AND ADENOSINE DIPHOSPHATE
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 | 5 |
| Details | BINDING SITE FOR RESIDUE MG A1553 |
| Chain | Residue |
| A | ASP452 |
| A | ASN479 |
| A | GLY481 |
| A | TZD1554 |
| A | HOH2353 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B1553 |
| Chain | Residue |
| B | HOH2262 |
| B | ASP452 |
| B | ASN479 |
| B | GLY481 |
| B | TZD1554 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TZD A1554 |
| 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 | MG1553 |
| A | HOH2353 |
| B | VAL32 |
| B | GLU56 |
| B | VAL79 |
| B | ASN86 |
| B | TYR120 |
| B | GLU121 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP A1555 |
| 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 | HOH2208 |
| A | HOH2354 |
| A | HOH2355 |
| A | HOH2356 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TZD B1554 |
| Chain | Residue |
| A | VAL32 |
| A | GLU56 |
| A | VAL79 |
| A | ASN86 |
| A | TYR120 |
| 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 | MG1553 |
| B | HOH2262 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP B1555 |
| Chain | Residue |
| B | ARG160 |
| B | GLY221 |
| B | LYS222 |
| B | GLY223 |
| B | MET247 |
| B | GLY280 |
| B | ALA281 |
| B | ARG282 |
| B | LEU286 |
| B | ASP306 |
| B | ILE307 |
| B | GLY324 |
| B | ASP325 |
| B | ILE326 |
| B | HOH2299 |
| B | HOH2300 |
| B | HOH2301 |
| B | HOH2302 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | VAL551 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | VAL551 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | PRO547 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | PRO547 |
