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3PX1

Structure of Calcium Binding Protein-1 from Entamoeba histolytica in complex with Strontium

Functional Information from GO Data
ChainGOidnamespacecontents
A0001891cellular_componentphagocytic cup
A0003779molecular_functionactin binding
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005737cellular_componentcytoplasm
A0006909biological_processphagocytosis
A0031143cellular_componentpseudopodium
A0032231biological_processregulation of actin filament bundle assembly
A0042995cellular_componentcell projection
A0045859biological_processregulation of protein kinase activity
A0046872molecular_functionmetal ion binding
A0050766biological_processpositive regulation of phagocytosis
A0051015molecular_functionactin filament binding
A1905303biological_processpositive regulation of macropinocytosis
B0001891cellular_componentphagocytic cup
B0003779molecular_functionactin binding
B0003785molecular_functionactin monomer binding
B0005509molecular_functioncalcium ion binding
B0005737cellular_componentcytoplasm
B0006909biological_processphagocytosis
B0031143cellular_componentpseudopodium
B0032231biological_processregulation of actin filament bundle assembly
B0042995cellular_componentcell projection
B0045859biological_processregulation of protein kinase activity
B0046872molecular_functionmetal ion binding
B0050766biological_processpositive regulation of phagocytosis
B0051015molecular_functionactin filament binding
B1905303biological_processpositive regulation of macropinocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SR A 149
ChainResidue
AASP10
AASN12
AASP14
AALA16
AGLU21

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SR A 150
ChainResidue
AGLU57
AASP46
AASP48
AASN50
AGLU52

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SR B 149
ChainResidue
BASP10
BASN12
BASP14
BALA16
BGLU21

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SR B 150
ChainResidue
BASP46
BASP48
BASN50
BGLU52
BGLU57

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DVNGDGAVSyeEV
ChainResidueDetails
AASP10-VAL22
AASP46-PHE58
AASP85-VAL97
AASP117-PHE129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: 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
ChainResidueDetails
AASP10
AGLU57
BASP10
BASN12
BASP14
BALA16
BGLU21
BASP46
BASP48
BASN50
BGLU52
AASN12
BGLU57
AASP14
AALA16
AGLU21
AASP46
AASP48
AASN50
AGLU52

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23782698, ECO:0007744|PDB:2M7N
ChainResidueDetails
AASP85
AASP87
AASP89
BASP85
BASP87
BASP89

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:11724551, ECO:0000269|PubMed:23782698, ECO:0007744|PDB:1JFK, ECO:0007744|PDB:2M7N
ChainResidueDetails
ALYS91
BASP117
BASN119
BASP121
BTYR123
BGLU128
AGLU96
AASP117
AASN119
AASP121
ATYR123
AGLU128
BLYS91
BGLU96

223790

PDB entries from 2024-08-14

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