1Z2L
Crystal structure of Allantoate-amidohydrolase from E.coli K12 in complex with substrate Allantoate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000256 | biological_process | allantoin catabolic process |
A | 0005737 | cellular_component | cytoplasm |
A | 0006144 | biological_process | purine nucleobase metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009442 | biological_process | allantoin assimilation pathway |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
A | 0030145 | molecular_function | manganese ion binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047652 | molecular_function | allantoate deiminase activity |
B | 0000256 | biological_process | allantoin catabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0006144 | biological_process | purine nucleobase metabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009442 | biological_process | allantoin assimilation pathway |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
B | 0030145 | molecular_function | manganese ion binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047652 | molecular_function | allantoate deiminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 511 |
Chain | Residue |
A | HIS83 |
A | ASP94 |
A | HIS192 |
A | ZN512 |
A | HOH629 |
A | HOH631 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 512 |
Chain | Residue |
A | ZN511 |
A | HOH631 |
A | ASP94 |
A | GLU129 |
A | HIS384 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 513 |
Chain | Residue |
B | HIS83 |
B | ASP94 |
B | HIS192 |
B | ZN514 |
B | HOH590 |
B | HOH591 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 514 |
Chain | Residue |
B | ASP94 |
B | GLU129 |
B | GLN195 |
B | HIS384 |
B | ZN513 |
B | HOH591 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 513 |
Chain | Residue |
A | GLN215 |
A | ARG217 |
A | ARG290 |
A | ALA358 |
A | GLY359 |
B | HIS228 |
B | 1AL516 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 515 |
Chain | Residue |
B | GLN215 |
B | ARG217 |
B | ARG290 |
B | ALA358 |
B | GLY359 |
B | HOH534 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 1AL B 516 |
Chain | Residue |
A | ARG217 |
A | ARG290 |
A | HIS384 |
A | SO4513 |
B | HIS228 |
B | ASN277 |
B | VAL278 |
B | HOH552 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17362992, ECO:0007744|PDB:1Z2L |
Chain | Residue | Details |
A | HIS83 | |
A | HIS192 | |
A | ARG217 | |
B | HIS83 | |
B | HIS192 | |
B | ARG217 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17362992, ECO:0000305|PubMed:25020232, ECO:0007744|PDB:1Z2L, ECO:0007744|PDB:4PXD |
Chain | Residue | Details |
A | ASP94 | |
A | GLU129 | |
A | HIS384 | |
B | ASP94 | |
B | GLU129 | |
B | HIS384 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17362992, ECO:0000269|PubMed:25020232, ECO:0007744|PDB:1Z2L, ECO:0007744|PDB:4PXD |
Chain | Residue | Details |
A | ASN277 | |
A | ARG290 | |
B | ASN277 | |
B | ARG290 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
A | GLU128 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
B | GLU128 |