2Q27
Crystal structure of oxalyl-coA decarboxylase from Escherichia coli
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 |
| A | 0071468 | biological_process | cellular response to acidic pH |
| 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 |
| B | 0071468 | biological_process | cellular response to acidic pH |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1001 |
| Chain | Residue |
| A | ASP447 |
| A | ASN474 |
| A | GLY476 |
| A | HOH6012 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1002 |
| Chain | Residue |
| B | ASP447 |
| B | ASN474 |
| B | GLY476 |
| B | HOH6081 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2001 |
| Chain | Residue |
| A | SER246 |
| A | ARG264 |
| A | ARG403 |
| A | HOH6152 |
| A | MET245 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2002 |
| Chain | Residue |
| B | MET245 |
| B | SER246 |
| B | ARG264 |
| B | ARG403 |
| B | HOH6188 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2005 |
| Chain | Residue |
| B | ALA263 |
| B | PHE266 |
| B | HIS351 |
| B | ASN355 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2006 |
| Chain | Residue |
| A | PHE266 |
| A | HIS351 |
| A | GLN354 |
| A | ASN355 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2007 |
| Chain | Residue |
| B | ARG158 |
| B | LYS220 |
| B | GLY221 |
| B | GLY278 |
| B | ALA279 |
| B | ARG280 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2008 |
| Chain | Residue |
| A | LYS220 |
| A | GLY221 |
| A | GLY278 |
| A | ARG280 |
| A | HOH6204 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2009 |
| Chain | Residue |
| A | ARG158 |
| A | GLY278 |
| A | ARG280 |
| A | ASP302 |
| site_id | BC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP A 3001 |
| Chain | Residue |
| A | GLU54 |
| A | PRO80 |
| A | ASN84 |
| A | TYR372 |
| A | GLY395 |
| A | ALA396 |
| A | ASN397 |
| A | THR398 |
| A | GLY421 |
| A | MET423 |
| A | GLY446 |
| A | ASP447 |
| A | SER448 |
| A | ALA449 |
| A | PHE452 |
| A | ASN474 |
| A | GLY476 |
| A | ILE477 |
| A | TYR478 |
| A | HOH6012 |
| A | HOH6239 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TPP B 4001 |
| Chain | Residue |
| B | GLU54 |
| B | ASN84 |
| B | GLU119 |
| B | TYR372 |
| B | GLY395 |
| B | ALA396 |
| B | ASN397 |
| B | THR398 |
| B | GLY421 |
| B | MET423 |
| B | GLY446 |
| B | ASP447 |
| B | SER448 |
| B | ALA449 |
| B | PHE452 |
| B | ASN474 |
| B | GLY476 |
| B | ILE477 |
| B | TYR478 |
| B | HOH6081 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 5001 |
| Chain | Residue |
| B | GLY221 |
| B | ASP302 |
| B | ILE303 |
| B | ILE322 |
| B | HOH6139 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 5002 |
| Chain | Residue |
| A | GLY221 |
| A | TYR224 |
| A | SER225 |
| A | ILE303 |
| A | ILE322 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES A 6001 |
| Chain | Residue |
| A | ILE32 |
| A | PRO33 |
| A | THR35 |
| A | ASP36 |
| A | GLU549 |
| A | SER550 |
| A | GLY551 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES B 6002 |
| Chain | Residue |
| B | GLY31 |
| B | ILE32 |
| B | PRO33 |
| B | THR35 |
| B | ASP36 |
| B | GLU549 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20553497","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | GLY547 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | GLY547 |
