6R4X
Crystal structure of PPEP-1(E143A/Y178F) in complex with substrate peptide Ac-EVNPAVP-CONH2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0005576 | cellular_component | extracellular region |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0016787 | molecular_function | hydrolase 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 301 |
Chain | Residue |
A | HIS142 |
A | HIS146 |
A | GLU185 |
D | PRO122 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | HIS142 |
B | HIS146 |
B | GLU185 |
C | PRO122 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for Di-peptide ACE C 118 and GLU C 119 |
Chain | Residue |
B | SER119 |
B | HIS150 |
B | HOH477 |
C | VAL120 |
C | ASN121 |
B | GLY118 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for Di-peptide VAL C 124 and LPD C 125 |
Chain | Residue |
A | GLU104 |
A | GLY105 |
B | GLY102 |
B | TRP103 |
B | HIS134 |
B | ASP135 |
B | ALA136 |
B | HIS142 |
B | ASN175 |
B | PHE178 |
B | HOH401 |
B | HOH487 |
C | ALA123 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for Di-peptide ACE D 118 and GLU D 119 |
Chain | Residue |
A | GLY118 |
A | SER119 |
A | HIS150 |
A | ASP155 |
A | LYS158 |
A | GLN198 |
A | HOH422 |
D | VAL120 |
D | ASN121 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for Di-peptide VAL D 124 and LPD D 125 |
Chain | Residue |
A | GLY102 |
A | TRP103 |
A | HIS134 |
A | ASP135 |
A | ALA136 |
A | HIS142 |
A | PHE178 |
A | HOH406 |
D | ALA123 |
D | HOH203 |
D | HOH204 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 370 |
Details | Domain: {"description":"ATLF-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01339","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Region: {"description":"Interacts with substrate peptide","evidences":[{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24303041","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01339","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Site: {"description":"Interacts with substrate peptide","evidences":[{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"26211609","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |