4TNU
Human brain aspartoacylase mutant Y231C complex with intermediate analog (N-phosphonomethyl-L-aspartate)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006083 | biological_process | acetate metabolic process |
A | 0006531 | biological_process | aspartate metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
A | 0019807 | molecular_function | aspartoacylase activity |
A | 0022010 | biological_process | central nervous system myelination |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0048714 | biological_process | positive regulation of oligodendrocyte differentiation |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006083 | biological_process | acetate metabolic process |
B | 0006531 | biological_process | aspartate metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
B | 0019807 | molecular_function | aspartoacylase activity |
B | 0022010 | biological_process | central nervous system myelination |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0048714 | biological_process | positive regulation of oligodendrocyte differentiation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | HIS21 |
A | GLU24 |
A | HIS116 |
A | AS9402 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue AS9 A 402 |
Chain | Residue |
A | HIS116 |
A | ASN117 |
A | ILE127 |
A | TYR164 |
A | ARG168 |
A | GLU178 |
A | GLU285 |
A | TYR288 |
A | ZN401 |
A | HIS21 |
A | GLU24 |
A | ARG63 |
A | ASN70 |
A | ARG71 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | HIS21 |
B | GLU24 |
B | HIS116 |
B | AS9402 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue AS9 B 402 |
Chain | Residue |
B | HIS21 |
B | GLU24 |
B | ARG63 |
B | ASN70 |
B | ARG71 |
B | HIS116 |
B | ASN117 |
B | TYR164 |
B | ARG168 |
B | GLU178 |
B | GLU285 |
B | TYR288 |
B | ZN401 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17027983, ECO:0000305|PubMed:18293939, ECO:0007744|PDB:2O4H |
Chain | Residue | Details |
A | GLU178 | |
B | GLU178 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 |
Chain | Residue | Details |
A | HIS21 | |
A | GLU24 | |
A | HIS116 | |
B | HIS21 | |
B | GLU24 | |
B | HIS116 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H |
Chain | Residue | Details |
A | ARG63 | |
B | TYR288 | |
A | ASN70 | |
A | TYR164 | |
A | ARG168 | |
A | TYR288 | |
B | ARG63 | |
B | ASN70 | |
B | TYR164 | |
B | ARG168 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 |
Chain | Residue | Details |
A | ARG71 | |
B | ARG71 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:17027983, ECO:0000305|PubMed:18293939, ECO:0007744|PDB:2O4H |
Chain | Residue | Details |
A | ARG63 | |
B | ARG63 |