5A0P
Apo-structure of metalloprotease Zmp1 from Clostridium difficile
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0005576 | cellular_component | extracellular region |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1221 |
Chain | Residue |
A | HIS142 |
A | HIS146 |
A | GLU185 |
A | HOH2191 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1221 |
Chain | Residue |
B | HIS142 |
B | HIS146 |
B | GLU185 |
B | HOH2182 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000305|PubMed:24303041, ECO:0000305|PubMed:26211609 |
Chain | Residue | Details |
A | GLU143 | |
B | GLU143 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:26211609 |
Chain | Residue | Details |
A | HIS142 | |
A | HIS146 | |
A | GLU185 | |
B | HIS142 | |
B | HIS146 | |
B | GLU185 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339 |
Chain | Residue | Details |
A | TYR178 | |
B | TYR178 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Interacts with substrate peptide => ECO:0000269|PubMed:26211609 |
Chain | Residue | Details |
A | ASP135 | |
A | HIS142 | |
B | ASP135 | |
B | HIS142 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:26211609 |
Chain | Residue | Details |
A | TYR178 | |
B | TYR178 |