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 | 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 | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:7578088 |
| Chain | Residue | Details |
| A | ILE294 | |
| A | LEU368 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:7619821, ECO:0007744|PDB:1LCP |
| Chain | Residue | Details |
| A | ILE202 | |
| A | ARG203 | |
| A | LYS205 | |
| A | 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 |
| A | SER282 | |
| A | ALA287 | |
| A | ASN305 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LCP |
| Chain | Residue | Details |
| A | 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 |
| A | 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 |
| A | 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 |
| A | ILE366 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q68FS4 |
| Chain | Residue | Details |
| A | SER42 | |
| A | PHE54 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPY7 |
| Chain | Residue | Details |
| A | PRO45 | |
| A | PHE61 | |
| A | LEU103 | |
| A | ILE476 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CPY7 |
| Chain | Residue | Details |
| A | PRO180 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P28838 |
| Chain | Residue | Details |
| A | ALA194 | |
| A | PRO238 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPY7 |
| Chain | Residue | Details |
| A | THR455 |
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 | ILE294 | electrostatic stabiliser |
| A | LEU368 | electrostatic stabiliser |
