4PXC
The crystal structure of AtUAH in complex with (S)-hydroxyglycine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000256 | biological_process | allantoin catabolic process |
| A | 0004848 | molecular_function | ureidoglycolate hydrolase activity |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| A | 0006145 | biological_process | purine nucleobase catabolic process |
| A | 0009536 | cellular_component | plastid |
| A | 0010136 | biological_process | ureide catabolic process |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0047652 | molecular_function | allantoate deiminase activity |
| B | 0000256 | biological_process | allantoin catabolic process |
| B | 0004848 | molecular_function | ureidoglycolate hydrolase activity |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0006144 | biological_process | purine nucleobase metabolic process |
| B | 0006145 | biological_process | purine nucleobase catabolic process |
| B | 0009536 | cellular_component | plastid |
| B | 0010136 | biological_process | ureide catabolic process |
| 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 | 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 MN A 501 |
| Chain | Residue |
| A | HIS138 |
| A | ASP149 |
| A | HIS254 |
| A | HOH613 |
| A | HOH732 |
| A | HOH787 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 502 |
| Chain | Residue |
| A | HGY503 |
| A | HOH689 |
| A | HOH732 |
| A | ASP149 |
| A | GLU184 |
| A | HIS448 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HGY A 503 |
| Chain | Residue |
| A | GLU184 |
| A | ARG353 |
| A | ALA422 |
| A | TYR423 |
| A | HIS448 |
| A | MN502 |
| A | HOH689 |
| A | HOH732 |
| B | HIS290 |
| B | ASN340 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MN B 501 |
| Chain | Residue |
| B | HIS138 |
| B | ASP149 |
| B | GLY150 |
| B | HIS254 |
| B | MN502 |
| B | HOH621 |
| B | HOH760 |
| B | HOH1080 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 502 |
| Chain | Residue |
| B | ASP149 |
| B | GLU184 |
| B | HIS448 |
| B | MN501 |
| B | HGY503 |
| B | HOH760 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HGY B 503 |
| Chain | Residue |
| A | HIS290 |
| A | ASN340 |
| B | GLU184 |
| B | ARG353 |
| B | ALA422 |
| B | TYR423 |
| B | HIS448 |
| B | MN502 |
| B | HOH760 |
| B | HOH1080 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE |
| Chain | Residue | Details |
| A | HIS138 | |
| B | ASP149 | |
| B | ALA183 | |
| B | GLU184 | |
| B | HIS254 | |
| B | ASN340 | |
| B | ARG353 | |
| B | TYR423 | |
| A | ASP149 | |
| A | ALA183 | |
| A | GLU184 | |
| A | HIS254 | |
| A | ASN340 | |
| A | ARG353 | |
| A | TYR423 | |
| B | HIS138 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB |
| Chain | Residue | Details |
| A | HIS290 | |
| B | HIS290 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC |
| Chain | Residue | Details |
| A | HIS448 | |
| B | HIS448 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Necessary for dimerization => ECO:0000250|UniProtKB:Q53389 |
| Chain | Residue | Details |
| A | ARG299 | |
| B | ARG299 |
