2Q29
Crystal structure of oxalyl-coA decarboxylase from Escherichia coli in complex with acetyl coenzyme A
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 | HOH4003 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1002 |
| Chain | Residue |
| B | ASP447 |
| B | ASN474 |
| B | GLY476 |
| B | HOH4002 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ACO A 2003 |
| Chain | Residue |
| A | ALA262 |
| A | ALA263 |
| A | ARG264 |
| A | SER265 |
| A | ASN355 |
| A | MET359 |
| A | ARG403 |
| A | ASN404 |
| A | HOH4030 |
| A | HOH4066 |
| A | HOH4145 |
| A | HOH4160 |
| A | HOH4239 |
| A | HOH4308 |
| A | HOH4353 |
| A | ALA261 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ACO B 3003 |
| Chain | Residue |
| B | ALA261 |
| B | ALA262 |
| B | ALA263 |
| B | ARG264 |
| B | SER265 |
| B | ASN355 |
| B | MET359 |
| B | ARG403 |
| B | ASN404 |
| B | HOH4049 |
| B | HOH4079 |
| B | HOH4159 |
| B | HOH4208 |
| B | HOH4220 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP A 2001 |
| 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 | HOH4003 |
| A | HOH4088 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP B 3001 |
| Chain | Residue |
| B | GLU54 |
| B | PRO80 |
| B | ASN84 |
| 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 | HOH4002 |
| B | HOH4257 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES B 4001 |
| Chain | Residue |
| B | GLY31 |
| B | ILE32 |
| B | PRO33 |
| B | THR35 |
| B | ASP36 |
| B | GLU549 |
| B | SER550 |
| B | HOH4083 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 4002 |
| Chain | Residue |
| A | GLY31 |
| A | ILE32 |
| A | PRO33 |
| A | THR35 |
| A | ASP36 |
| A | GLU549 |
| A | SER550 |
| A | HOH4097 |
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 |
