4H8A
Crystal structure of ureidoglycolate dehydrogenase in binary complex with NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000256 | biological_process | allantoin catabolic process |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| A | 0009040 | molecular_function | ureidoglycolate dehydrogenase activity |
| A | 0009442 | biological_process | allantoin assimilation pathway |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0000256 | biological_process | allantoin catabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006144 | biological_process | purine nucleobase metabolic process |
| B | 0009040 | molecular_function | ureidoglycolate dehydrogenase activity |
| B | 0009442 | biological_process | allantoin assimilation pathway |
| B | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAI A 401 |
| Chain | Residue |
| A | ILE41 |
| A | ASP174 |
| A | ALA176 |
| A | ALA181 |
| A | TYR303 |
| A | TYR304 |
| A | GLY306 |
| A | ASP308 |
| A | GLN309 |
| A | HOH522 |
| A | HOH523 |
| A | HIS44 |
| A | HOH525 |
| A | HOH526 |
| A | HOH533 |
| A | HOH547 |
| A | HOH550 |
| A | HOH577 |
| A | HOH589 |
| A | HOH614 |
| A | HOH616 |
| A | HOH633 |
| A | HIS116 |
| A | HOH690 |
| A | HOH710 |
| A | HOH754 |
| B | PHE147 |
| B | PRO223 |
| B | LYS224 |
| A | GLY118 |
| A | ILE120 |
| A | SER140 |
| A | THR156 |
| A | PRO158 |
| A | PHE173 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAI B 401 |
| Chain | Residue |
| A | PHE147 |
| A | PRO223 |
| A | LYS224 |
| A | HOH544 |
| A | HOH660 |
| B | HIS44 |
| B | HIS116 |
| B | GLY118 |
| B | ILE120 |
| B | SER140 |
| B | THR156 |
| B | PRO158 |
| B | PHE173 |
| B | ASP174 |
| B | ALA176 |
| B | ALA181 |
| B | TYR303 |
| B | TYR304 |
| B | PRO305 |
| B | GLY306 |
| B | ASP308 |
| B | GLN309 |
| B | HOH511 |
| B | HOH528 |
| B | HOH560 |
| B | HOH653 |
| B | HOH667 |
| B | HOH670 |
| B | HOH722 |
| B | HOH749 |
| B | HOH752 |
| B | HOH798 |
| B | HOH848 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23284870","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23284870","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4H8A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Plays a crucial role in stabilizing the binding of (S)-ureidoglycolate","evidences":[{"source":"PubMed","id":"23284870","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
