2AQV
Crystal Structure of E. coli Isoaspartyl Dipeptidase mutant Y137F
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 801 |
Chain | Residue |
A | HIS68 |
A | HIS70 |
A | KCX162 |
A | ASP285 |
A | ZN802 |
A | HOH910 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 802 |
Chain | Residue |
A | ZN801 |
A | HOH910 |
A | KCX162 |
A | HIS201 |
A | HIS230 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 803 |
Chain | Residue |
B | HIS68 |
B | HIS70 |
B | KCX162 |
B | ASP285 |
B | ZN804 |
B | HOH981 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 804 |
Chain | Residue |
B | KCX162 |
B | HIS201 |
B | HIS230 |
B | ZN803 |
B | HOH981 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:12946361 |
Chain | Residue | Details |
A | ASP285 | |
B | ASP285 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685 |
Chain | Residue | Details |
A | HIS68 | |
B | ASP285 | |
A | HIS70 | |
A | HIS201 | |
A | HIS230 | |
A | ASP285 | |
B | HIS68 | |
B | HIS70 | |
B | HIS201 | |
B | HIS230 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY75 | |
B | GLY75 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12718528, ECO:0000305|PubMed:12946361, ECO:0000305|PubMed:15882050 |
Chain | Residue | Details |
A | THR106 | |
B | SER289 | |
A | PHE137 | |
A | ARG169 | |
A | ARG233 | |
A | SER289 | |
B | THR106 | |
B | PHE137 | |
B | ARG169 | |
B | ARG233 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685 |
Chain | Residue | Details |
A | KCX162 | |
B | KCX162 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685 |
Chain | Residue | Details |
A | KCX162 | |
B | KCX162 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 172 |
Chain | Residue | Details |
A | HIS68 | metal ligand |
A | HIS70 | metal ligand |
A | KCX162 | metal ligand |
A | HIS201 | metal ligand |
A | HIS230 | metal ligand |
A | ASP285 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 172 |
Chain | Residue | Details |
B | HIS68 | metal ligand |
B | HIS70 | metal ligand |
B | KCX162 | metal ligand |
B | HIS201 | metal ligand |
B | HIS230 | metal ligand |
B | ASP285 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |