3QJK
Structure of Calcium Binding Protein-1 from Entamoeba histolytica in complex with Lead
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001891 | cellular_component | phagocytic cup |
A | 0003779 | molecular_function | actin binding |
A | 0003785 | molecular_function | actin monomer binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006909 | biological_process | phagocytosis |
A | 0031143 | cellular_component | pseudopodium |
A | 0032231 | biological_process | regulation of actin filament bundle assembly |
A | 0042995 | cellular_component | cell projection |
A | 0045859 | biological_process | regulation of protein kinase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050766 | biological_process | positive regulation of phagocytosis |
A | 0051015 | molecular_function | actin filament binding |
A | 1905303 | biological_process | positive regulation of macropinocytosis |
B | 0001891 | cellular_component | phagocytic cup |
B | 0003779 | molecular_function | actin binding |
B | 0003785 | molecular_function | actin monomer binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006909 | biological_process | phagocytosis |
B | 0031143 | cellular_component | pseudopodium |
B | 0032231 | biological_process | regulation of actin filament bundle assembly |
B | 0042995 | cellular_component | cell projection |
B | 0045859 | biological_process | regulation of protein kinase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050766 | biological_process | positive regulation of phagocytosis |
B | 0051015 | molecular_function | actin filament binding |
B | 1905303 | biological_process | positive regulation of macropinocytosis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PB A 201 |
Chain | Residue |
A | ASP10 |
A | ASN12 |
A | ASP14 |
A | ALA16 |
A | GLU21 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PB A 202 |
Chain | Residue |
A | GLU57 |
A | ASP46 |
A | ASP48 |
A | ASN50 |
A | GLU52 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACT A 203 |
Chain | Residue |
A | TYR62 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PB B 201 |
Chain | Residue |
B | ASP10 |
B | ASN12 |
B | ASP14 |
B | ALA16 |
B | GLU21 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PB B 202 |
Chain | Residue |
B | ASP46 |
B | ASP48 |
B | ASN50 |
B | GLU52 |
B | GLU57 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DVNGDGAVSyeEV |
Chain | Residue | Details |
A | ASP10-VAL22 | |
A | ASP46-PHE58 | |
A | ASP85-VAL97 | |
A | ASP117-PHE129 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11724551, ECO:0000269|PubMed:17554780, ECO:0000269|PubMed:20550906, ECO:0000269|PubMed:23782698, ECO:0000305|PubMed:22906057, ECO:0007744|PDB:1JFK, ECO:0007744|PDB:2M7M, ECO:0007744|PDB:2NXQ, ECO:0007744|PDB:3LI6, ECO:0007744|PDB:3PX1, ECO:0007744|PDB:3QJK, ECO:0007744|PDB:3ULG |
Chain | Residue | Details |
A | ASP10 | |
A | GLU57 | |
B | ASP10 | |
B | ASN12 | |
B | ASP14 | |
B | ALA16 | |
B | GLU21 | |
B | ASP46 | |
B | ASP48 | |
B | ASN50 | |
B | GLU52 | |
A | ASN12 | |
B | GLU57 | |
A | ASP14 | |
A | ALA16 | |
A | GLU21 | |
A | ASP46 | |
A | ASP48 | |
A | ASN50 | |
A | GLU52 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23782698, ECO:0007744|PDB:2M7N |
Chain | Residue | Details |
A | ASP85 | |
A | ASP87 | |
A | ASP89 | |
B | ASP85 | |
B | ASP87 | |
B | ASP89 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11724551, ECO:0000269|PubMed:23782698, ECO:0007744|PDB:1JFK, ECO:0007744|PDB:2M7N |
Chain | Residue | Details |
A | LYS91 | |
B | ASP117 | |
B | ASN119 | |
B | ASP121 | |
B | TYR123 | |
B | GLU128 | |
A | GLU96 | |
A | ASP117 | |
A | ASN119 | |
A | ASP121 | |
A | TYR123 | |
A | GLU128 | |
B | LYS91 | |
B | GLU96 |