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 | 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 |
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 | 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 |
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 | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ILE32 | |
A | TYR118 | |
A | SER550 | |
B | ILE32 | |
B | TYR118 | |
B | SER550 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20553497 |
Chain | Residue | Details |
A | ARG158 | |
A | TYR478 | |
B | ARG158 | |
B | LYS220 | |
B | ARG280 | |
B | ASP302 | |
B | ILE322 | |
B | TYR372 | |
B | ASP447 | |
B | ASN474 | |
B | GLY476 | |
A | LYS220 | |
B | TYR478 | |
A | ARG280 | |
A | ASP302 | |
A | ILE322 | |
A | TYR372 | |
A | ASP447 | |
A | ASN474 | |
A | GLY476 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ALA261 | |
B | ALA261 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN355 | |
B | SER448 | |
A | ALA396 | |
A | ARG403 | |
A | GLY421 | |
A | SER448 | |
B | ASN355 | |
B | ALA396 | |
B | ARG403 | |
B | GLY421 |
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 |