2Q28
Crystal structure of oxalyl-coA decarboxylase from Escherichia coli in complex with adenosine-5`-diphosphate
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 | 0005777 | cellular_component | peroxisome |
| A | 0008949 | molecular_function | oxalyl-CoA decarboxylase activity |
| A | 0016829 | molecular_function | lyase 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 | 0005777 | cellular_component | peroxisome |
| B | 0008949 | molecular_function | oxalyl-CoA decarboxylase activity |
| B | 0016829 | molecular_function | lyase 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 | HOH4057 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1002 |
| Chain | Residue |
| B | ASP447 |
| B | ASN474 |
| B | GLY476 |
| B | HOH5088 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2001 |
| Chain | Residue |
| A | TYR478 |
| A | SER550 |
| A | HOH4085 |
| A | HOH4115 |
| A | HOH4174 |
| A | HOH4371 |
| A | HOH4467 |
| A | TYR118 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2002 |
| Chain | Residue |
| B | TYR118 |
| B | TYR478 |
| B | SER550 |
| B | HOH5158 |
| B | HOH5171 |
| B | HOH5302 |
| B | HOH5373 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP A 4001 |
| 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 | HOH4057 |
| A | HOH4174 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP A 4003 |
| Chain | Residue |
| A | ARG158 |
| A | GLY219 |
| A | LYS220 |
| A | GLY221 |
| A | TYR224 |
| A | MET245 |
| A | GLY278 |
| A | ALA279 |
| A | ARG280 |
| A | LEU284 |
| A | ASP302 |
| A | ILE303 |
| A | GLY320 |
| A | ASP321 |
| A | ILE322 |
| A | HOH4029 |
| A | HOH4031 |
| A | HOH4052 |
| A | HOH4072 |
| A | HOH4272 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MES A 4004 |
| Chain | Residue |
| A | ILE32 |
| A | PRO33 |
| A | THR35 |
| A | ASP36 |
| A | GLU549 |
| A | SER550 |
| A | GLY551 |
| A | HIS552 |
| A | ILE553 |
| A | HOH4080 |
| A | HOH4216 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP B 5001 |
| 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 | HOH5088 |
| B | HOH5302 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP B 5003 |
| Chain | Residue |
| B | GLY221 |
| B | MET245 |
| B | GLY278 |
| B | ALA279 |
| B | ARG280 |
| B | LEU284 |
| B | ASP302 |
| B | ILE303 |
| B | GLU304 |
| B | GLY320 |
| B | ASP321 |
| B | ILE322 |
| B | HOH5026 |
| B | HOH5038 |
| B | HOH5066 |
| B | HOH5068 |
| B | HOH5322 |
| B | ARG158 |
| B | GLY219 |
| B | LYS220 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MES B 5004 |
| Chain | Residue |
| B | ILE32 |
| B | PRO33 |
| B | THR35 |
| B | ASP36 |
| B | GLU549 |
| B | SER550 |
| B | GLY551 |
| B | HIS552 |
| B | ILE553 |
| B | HOH5086 |
| B | HOH5424 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 3001 |
| Chain | Residue |
| A | ASN95 |
| A | GLY96 |
| A | PHE97 |
| A | PRO159 |
| A | LYS220 |
| A | GLY221 |
| A | TYR224 |
| A | HOH4093 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 3002 |
| Chain | Residue |
| B | ASN95 |
| B | GLY96 |
| B | PHE97 |
| B | PRO159 |
| B | LYS220 |
| B | TYR224 |
| B | HOH5079 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 3003 |
| Chain | Residue |
| A | GLN115 |
| A | HIS287 |
| A | LYS289 |
| A | ASN311 |
| A | HOH4062 |
| A | HOH4135 |
| A | HOH4187 |
| A | HOH4230 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 3004 |
| Chain | Residue |
| A | HOH4297 |
| B | THR182 |
| B | THR183 |
| B | HOH5025 |
| B | HOH5296 |
| B | HOH5420 |
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 |
