4PXD
The crystal structure of EcAAH in complex with 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 | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 501 |
| Chain | Residue |
| A | ASP92 |
| A | GLU127 |
| A | GLN193 |
| A | HIS382 |
| A | 1AL502 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 1AL A 502 |
| Chain | Residue |
| A | PHE135 |
| A | HIS190 |
| A | GLN193 |
| A | GLN213 |
| A | ARG215 |
| A | ARG288 |
| A | ALA356 |
| A | GLY357 |
| A | HIS358 |
| A | HIS382 |
| A | MN501 |
| B | HIS226 |
| B | ASN275 |
| A | ASP92 |
| A | ALA126 |
| A | GLU127 |
| A | VAL134 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 501 |
| Chain | Residue |
| B | ASP92 |
| B | GLU127 |
| B | GLN193 |
| B | HIS382 |
| B | 1AL502 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 1AL B 502 |
| Chain | Residue |
| A | HIS226 |
| A | ASN275 |
| B | ASP92 |
| B | ALA126 |
| B | GLU127 |
| B | VAL134 |
| B | PHE135 |
| B | HIS190 |
| B | GLN193 |
| B | GLN213 |
| B | ARG215 |
| B | ARG288 |
| B | ALA356 |
| B | GLY357 |
| B | HIS358 |
| B | HIS382 |
| B | MN501 |
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 | HIS81 | |
| A | HIS190 | |
| A | ARG215 | |
| B | HIS81 | |
| B | HIS190 | |
| B | ARG215 |
| 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 | ASP92 | |
| A | GLU127 | |
| A | HIS382 | |
| B | ASP92 | |
| B | GLU127 | |
| B | HIS382 |
| 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 | ASN275 | |
| A | ARG288 | |
| B | ASN275 | |
| B | ARG288 |
