3E74
Crystal structure of E. coli allantoinase with iron ions at the metal center
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000256 | biological_process | allantoin catabolic process |
A | 0004038 | molecular_function | allantoinase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006144 | biological_process | purine nucleobase metabolic process |
A | 0006145 | biological_process | purine nucleobase catabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009442 | biological_process | allantoin assimilation pathway |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0046872 | molecular_function | metal ion binding |
A | 0050897 | molecular_function | cobalt ion binding |
B | 0000256 | biological_process | allantoin catabolic process |
B | 0004038 | molecular_function | allantoinase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006144 | biological_process | purine nucleobase metabolic process |
B | 0006145 | biological_process | purine nucleobase catabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009442 | biological_process | allantoin assimilation pathway |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0046872 | molecular_function | metal ion binding |
B | 0050897 | molecular_function | cobalt ion binding |
C | 0000256 | biological_process | allantoin catabolic process |
C | 0004038 | molecular_function | allantoinase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006144 | biological_process | purine nucleobase metabolic process |
C | 0006145 | biological_process | purine nucleobase catabolic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0009442 | biological_process | allantoin assimilation pathway |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
C | 0046872 | molecular_function | metal ion binding |
C | 0050897 | molecular_function | cobalt ion binding |
D | 0000256 | biological_process | allantoin catabolic process |
D | 0004038 | molecular_function | allantoinase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006144 | biological_process | purine nucleobase metabolic process |
D | 0006145 | biological_process | purine nucleobase catabolic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0009442 | biological_process | allantoin assimilation pathway |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
D | 0046872 | molecular_function | metal ion binding |
D | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 454 |
Chain | Residue |
A | HIS59 |
A | HIS61 |
A | KCX146 |
A | ASP315 |
A | FE455 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 455 |
Chain | Residue |
A | HOH456 |
A | KCX146 |
A | HIS186 |
A | HIS242 |
A | FE454 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE B 454 |
Chain | Residue |
B | KCX146 |
B | HIS186 |
B | HIS242 |
B | FE455 |
B | HOH684 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE B 455 |
Chain | Residue |
B | HIS59 |
B | HIS61 |
B | KCX146 |
B | ASP315 |
B | FE454 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE C 454 |
Chain | Residue |
C | KCX146 |
C | HIS186 |
C | HIS242 |
C | FE455 |
C | HOH531 |
C | HOH722 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE C 455 |
Chain | Residue |
C | HIS59 |
C | HIS61 |
C | KCX146 |
C | ASP315 |
C | FE454 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE D 454 |
Chain | Residue |
D | KCX146 |
D | HIS186 |
D | HIS242 |
D | FE455 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE D 455 |
Chain | Residue |
D | HIS59 |
D | HIS61 |
D | KCX146 |
D | ASP315 |
D | FE454 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS59 | |
B | ASP315 | |
C | HIS59 | |
C | HIS61 | |
C | HIS186 | |
C | HIS242 | |
C | ASP315 | |
D | HIS59 | |
D | HIS61 | |
D | HIS186 | |
D | HIS242 | |
A | HIS61 | |
D | ASP315 | |
A | HIS186 | |
A | HIS242 | |
A | ASP315 | |
B | HIS59 | |
B | HIS61 | |
B | HIS186 | |
B | HIS242 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: via carbamate group => ECO:0000250 |
Chain | Residue | Details |
A | KCX146 | |
B | KCX146 | |
C | KCX146 | |
D | KCX146 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-carboxylysine => ECO:0000250 |
Chain | Residue | Details |
A | KCX146 | |
B | KCX146 | |
C | KCX146 | |
D | KCX146 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
A | ASP315 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
B | ASP315 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
C | ASP315 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
D | ASP315 |