1BLL
X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0004177 | molecular_function | aminopeptidase activity |
E | 0004180 | molecular_function | carboxypeptidase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0005739 | cellular_component | mitochondrion |
E | 0006508 | biological_process | proteolysis |
E | 0008233 | molecular_function | peptidase activity |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016805 | molecular_function | dipeptidase activity |
E | 0019538 | biological_process | protein metabolic process |
E | 0030145 | molecular_function | manganese ion binding |
E | 0046872 | molecular_function | metal ion binding |
E | 0070006 | molecular_function | metalloaminopeptidase activity |
E | 0097718 | molecular_function | disordered domain specific binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 488 |
Chain | Residue |
E | ASP255 |
E | ASP332 |
E | GLU334 |
E | ZN489 |
I | L2O2 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN E 489 |
Chain | Residue |
E | ZN488 |
I | L2O2 |
E | LYS250 |
E | ASP255 |
E | ASP273 |
E | GLU334 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR CHAIN I OF AMASTATIN |
Chain | Residue |
E | LYS250 |
E | ASP255 |
E | LYS262 |
E | MET270 |
E | ASP273 |
E | ASP332 |
E | GLU334 |
E | ARG336 |
E | THR359 |
E | LEU360 |
E | GLY362 |
E | ALA363 |
E | ILE366 |
E | ILE366 |
E | ARG425 |
E | GLY428 |
E | ZN488 |
E | ZN489 |
E | HOH594 |
Functional Information from PROSITE/UniProt
site_id | PS00631 |
Number of Residues | 8 |
Details | CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL |
Chain | Residue | Details |
E | 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 | 4 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CPY7","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68FS4","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 |
E | LYS262 | |
E | ARG336 | |
E | ASP255 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 587 |
Chain | Residue | Details |