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 | 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 | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:7578088 |
Chain | Residue | Details |
E | ILE294 | |
E | LEU368 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:7619821, ECO:0007744|PDB:1LCP |
Chain | Residue | Details |
E | ILE202 | |
E | ARG203 | |
E | LYS205 | |
E | CYS303 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A |
Chain | Residue | Details |
E | SER282 | |
E | ALA287 | |
E | ASN305 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LCP |
Chain | Residue | Details |
E | LEU292 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7578088, ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LAN, ECO:0007744|PDB:1LCP |
Chain | Residue | Details |
E | ILE294 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A |
Chain | Residue | Details |
E | MET364 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345, ECO:0007744|PDB:1BPM, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A |
Chain | Residue | Details |
E | ILE366 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q68FS4 |
Chain | Residue | Details |
E | SER42 | |
E | PHE54 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPY7 |
Chain | Residue | Details |
E | PRO45 | |
E | PHE61 | |
E | LEU103 | |
E | ILE476 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CPY7 |
Chain | Residue | Details |
E | PRO180 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P28838 |
Chain | Residue | Details |
E | ALA194 | |
E | PRO238 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPY7 |
Chain | Residue | Details |
E | THR455 |
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 |
E | ILE294 | electrostatic stabiliser |
E | LEU368 | electrostatic stabiliser |