2Q4Z
Ensemble refinement of the protein crystal structure of an aspartoacylase from Rattus norvegicus
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 601 |
Chain | Residue |
A | HIS20 |
A | GLU23 |
A | HIS115 |
A | HOH748 |
A | HOH778 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 701 |
Chain | Residue |
A | TYR163 |
A | HOH834 |
B | ARG308 |
B | THR310 |
A | ASP73 |
A | LEU74 |
A | LYS102 |
A | ASN103 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 702 |
Chain | Residue |
A | ARG196 |
A | LYS199 |
A | HIS200 |
A | HOH962 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 703 |
Chain | Residue |
A | THR61 |
A | HOH779 |
A | HOH795 |
A | HOH836 |
A | HOH969 |
A | HOH988 |
B | THR61 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 602 |
Chain | Residue |
B | HIS20 |
B | GLU23 |
B | ARG62 |
B | HIS115 |
B | HOH733 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 704 |
Chain | Residue |
B | ASP67 |
B | ASN69 |
B | TYR287 |
B | HOH878 |
B | HOH927 |
B | HOH943 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 705 |
Chain | Residue |
B | ARG196 |
B | LYS199 |
B | HIS200 |
B | HOH763 |
B | HOH922 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P45381 |
Chain | Residue | Details |
A | GLU177 | |
B | GLU177 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17194761, ECO:0007744|PDB:2GU2 |
Chain | Residue | Details |
A | HIS20 | |
A | GLU23 | |
A | HIS115 | |
B | HIS20 | |
B | GLU23 | |
B | HIS115 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P45381 |
Chain | Residue | Details |
A | ARG62 | |
B | ARG167 | |
B | TYR287 | |
A | ARG70 | |
A | TYR163 | |
A | ARG167 | |
A | TYR287 | |
B | ARG62 | |
B | ASN69 | |
B | ARG70 | |
B | TYR163 | |
A | ASN69 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P45381 |
Chain | Residue | Details |
A | ARG62 | |
B | ARG62 |