4PXE
The crystal structure of AtUAH in complex with glyoxylate
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 | HOH608 |
A | HOH621 |
A | HOH648 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 502 |
Chain | Residue |
A | GLV503 |
A | HOH621 |
B | HOH615 |
A | ASP149 |
A | GLU184 |
A | HIS448 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLV A 503 |
Chain | Residue |
A | GLU183 |
A | GLU184 |
A | ARG353 |
A | ALA422 |
A | TYR423 |
A | HIS448 |
A | MN502 |
A | HOH621 |
B | HIS290 |
B | ASN340 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 501 |
Chain | Residue |
B | HIS138 |
B | ASP149 |
B | HIS254 |
B | HOH621 |
B | HOH638 |
B | HOH672 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 502 |
Chain | Residue |
A | HOH1238 |
B | ASP149 |
B | GLU184 |
B | HIS448 |
B | GLV503 |
B | HOH638 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLV B 503 |
Chain | Residue |
A | HIS290 |
A | ASN340 |
B | GLU183 |
B | GLU184 |
B | ARG353 |
B | ALA422 |
B | TYR423 |
B | HIS448 |
B | MN502 |
B | HOH638 |
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 | GLU183 | |
B | GLU184 | |
B | HIS254 | |
B | ASN340 | |
B | ARG353 | |
B | TYR423 | |
A | ASP149 | |
A | GLU183 | |
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 |