1LCP
BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH L-LEUCINE PHOSPHONIC ACID
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 |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0004180 | molecular_function | carboxypeptidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016805 | molecular_function | dipeptidase activity |
| B | 0019538 | biological_process | protein metabolic process |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070006 | molecular_function | metalloaminopeptidase activity |
| B | 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 A 488 |
| Chain | Residue |
| A | ASP255 |
| A | ASP332 |
| A | GLU334 |
| A | ZN489 |
| A | PLU500 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 489 |
| Chain | Residue |
| A | LYS250 |
| A | ASP255 |
| A | ASP273 |
| A | GLU334 |
| A | ZN488 |
| A | PLU500 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 490 |
| Chain | Residue |
| A | LEU170 |
| A | MET171 |
| A | THR173 |
| A | ARG271 |
| A | MET274 |
| A | HOH525 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 488 |
| Chain | Residue |
| B | ASP255 |
| B | ASP332 |
| B | GLU334 |
| B | ZN489 |
| B | PLU500 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 489 |
| Chain | Residue |
| B | LYS250 |
| B | ASP255 |
| B | ASP273 |
| B | GLU334 |
| B | ZN488 |
| B | PLU500 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 490 |
| Chain | Residue |
| B | LEU170 |
| B | MET171 |
| B | THR173 |
| B | ARG271 |
| B | MET274 |
| B | HOH588 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLU A 500 |
| Chain | Residue |
| A | LYS250 |
| A | ASP255 |
| A | LYS262 |
| A | ASP273 |
| A | ASP332 |
| A | GLU334 |
| A | THR359 |
| A | LEU360 |
| A | ALA451 |
| A | MET454 |
| A | ZN488 |
| A | ZN489 |
| A | HOH713 |
| A | HOH756 |
| A | HOH989 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLU B 500 |
| Chain | Residue |
| B | LYS250 |
| B | ASP255 |
| B | LYS262 |
| B | ASP273 |
| B | ASP332 |
| B | GLU334 |
| B | THR359 |
| B | LEU360 |
| B | ALA451 |
| B | ZN488 |
| B | ZN489 |
| B | HOH587 |
| B | HOH929 |
| B | HOH985 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD B 501 |
| Chain | Residue |
| B | TRP82 |
| B | ASN88 |
| B | HOH545 |
| B | HOH646 |
| B | HOH707 |
| B | HOH921 |
| site_id | ASA |
| Number of Residues | 11 |
| Details |
| Chain | Residue |
| A | GLU334 |
| A | THR361 |
| A | GLY362 |
| A | ASP255 |
| A | ASP332 |
| A | ASP273 |
| A | LYS250 |
| A | LYS262 |
| A | GLY335 |
| A | ARG336 |
| A | LEU360 |
| site_id | ASB |
| Number of Residues | 11 |
| Details |
| Chain | Residue |
| B | GLU334 |
| B | ASP255 |
| B | ASP332 |
| B | ASP273 |
| B | LYS250 |
| B | LYS262 |
| B | GLY335 |
| B | ARG336 |
| B | LEU360 |
| B | THR361 |
| B | GLY362 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD A 501 |
| Chain | Residue |
| A | TRP82 |
| A | ASN88 |
| A | HOH576 |
| A | HOH744 |
| A | HOH831 |
| B | HOH560 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD A 502 |
| Chain | Residue |
| A | ARG52 |
| A | HOH649 |
| B | ASP102 |
| A | LEU46 |
| A | THR51 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MRD B 502 |
| Chain | Residue |
| A | ASP102 |
| A | LEU103 |
| B | LEU46 |
| B | LYS50 |
| B | THR51 |
| B | ARG52 |
| B | HOH581 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MRD A 503 |
| Chain | Residue |
| A | HIS233 |
| A | PRO244 |
| A | ASN295 |
| A | ILE296 |
| A | VAL297 |
| A | HOH568 |
| A | HOH580 |
| A | HOH841 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MRD B 503 |
| Chain | Residue |
| B | ASN295 |
| B | ILE296 |
| B | HOH617 |
| B | HOH889 |
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 | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7578088","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| 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 | 6 |
| 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 | 2 |
| 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 | 2 |
| 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 | 2 |
| 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 | 2 |
| 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":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68FS4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CPY7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P28838","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| 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 | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1lam |
| Chain | Residue | Details |
| B | LYS262 | |
| B | ARG336 | |
| B | ASP255 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 587 |
| Chain | Residue | Details |
| A | LYS262 | electrostatic stabiliser |
| A | ARG336 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 587 |
| Chain | Residue | Details |
| B | LYS262 | electrostatic stabiliser |
| B | ARG336 | electrostatic stabiliser |






