1BPM
DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016805 | molecular_function | dipeptidase activity |
| A | 0019538 | biological_process | protein metabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070006 | molecular_function | metalloaminopeptidase activity |
| A | 0097718 | molecular_function | disordered domain specific binding |
Functional Information from PDB Data
| site_id | 488 |
| Number of Residues | 1 |
| Details | THE ZINC OF THE NATIVE ENZYME OF *SITE 1* IS READILY EXCHANGEABLE |
| Chain | Residue |
| A | MG488 |
| site_id | 489 |
| Number of Residues | 1 |
| Details | *SITE 2* BINDS THE ZINC MUCH MORE STRONGLY |
| Chain | Residue |
| A | ZN489 |
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 488 |
| Chain | Residue |
| A | ASP255 |
| A | ASP332 |
| A | GLU334 |
| A | ZN489 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 489 |
| Chain | Residue |
| A | GLU334 |
| A | MG488 |
| A | LYS250 |
| A | ASP255 |
| A | ASP273 |
Functional Information from PROSITE/UniProt
| site_id | PS00631 |
| Number of Residues | 8 |
| Details | CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL |
| Chain | Residue | Details |
| A | ASN330-LEU337 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7578088","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7619821","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LCP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16519517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17157838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2EWB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J9A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7619821","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LCP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7578088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7619821","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LAN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LCP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16519517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17157838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8506345","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2EWB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J9A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16519517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17157838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8506345","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2EWB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J9A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68FS4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CPY7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CPY7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P28838","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CPY7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1lam |
| Chain | Residue | Details |
| A | LYS262 | |
| A | ARG336 | |
| A | ASP255 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 587 |
| Chain | Residue | Details |
| A | LYS262 | electrostatic stabiliser |
| A | ARG336 | electrostatic stabiliser |
