Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4F7R

Crystal structure of 14-3-3 protein from Giardia intestinalis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000165	biological_process	MAPK cascade
A	0003779	molecular_function	actin binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005635	cellular_component	nuclear envelope
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005819	cellular_component	spindle
A	0005856	cellular_component	cytoskeleton
A	0005930	cellular_component	axoneme
A	0007165	biological_process	signal transduction
A	0008104	biological_process	protein localization
A	0019900	molecular_function	kinase binding
A	0030010	biological_process	establishment of cell polarity
A	0030036	biological_process	actin cytoskeleton organization
A	0031514	cellular_component	motile cilium
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0050815	molecular_function	phosphoserine residue binding
A	0051219	molecular_function	phosphoprotein binding
A	0051289	biological_process	protein homotetramerization
A	0051495	biological_process	positive regulation of cytoskeleton organization
A	0070207	biological_process	protein homotrimerization
A	0097298	biological_process	regulation of nucleus size
A	1990051	biological_process	activation of protein kinase C activity
B	0000165	biological_process	MAPK cascade
B	0003779	molecular_function	actin binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005635	cellular_component	nuclear envelope
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005819	cellular_component	spindle
B	0005856	cellular_component	cytoskeleton
B	0005930	cellular_component	axoneme
B	0007165	biological_process	signal transduction
B	0008104	biological_process	protein localization
B	0019900	molecular_function	kinase binding
B	0030010	biological_process	establishment of cell polarity
B	0030036	biological_process	actin cytoskeleton organization
B	0031514	cellular_component	motile cilium
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0050815	molecular_function	phosphoserine residue binding
B	0051219	molecular_function	phosphoprotein binding
B	0051289	biological_process	protein homotetramerization
B	0051495	biological_process	positive regulation of cytoskeleton organization
B	0070207	biological_process	protein homotrimerization
B	0097298	biological_process	regulation of nucleus size
B	1990051	biological_process	activation of protein kinase C activity
C	0000165	biological_process	MAPK cascade
C	0003779	molecular_function	actin binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005635	cellular_component	nuclear envelope
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005819	cellular_component	spindle
C	0005856	cellular_component	cytoskeleton
C	0005930	cellular_component	axoneme
C	0007165	biological_process	signal transduction
C	0008104	biological_process	protein localization
C	0019900	molecular_function	kinase binding
C	0030010	biological_process	establishment of cell polarity
C	0030036	biological_process	actin cytoskeleton organization
C	0031514	cellular_component	motile cilium
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0050815	molecular_function	phosphoserine residue binding
C	0051219	molecular_function	phosphoprotein binding
C	0051289	biological_process	protein homotetramerization
C	0051495	biological_process	positive regulation of cytoskeleton organization
C	0070207	biological_process	protein homotrimerization
C	0097298	biological_process	regulation of nucleus size
C	1990051	biological_process	activation of protein kinase C activity
D	0000165	biological_process	MAPK cascade
D	0003779	molecular_function	actin binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005635	cellular_component	nuclear envelope
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0005819	cellular_component	spindle
D	0005856	cellular_component	cytoskeleton
D	0005930	cellular_component	axoneme
D	0007165	biological_process	signal transduction
D	0008104	biological_process	protein localization
D	0019900	molecular_function	kinase binding
D	0030010	biological_process	establishment of cell polarity
D	0030036	biological_process	actin cytoskeleton organization
D	0031514	cellular_component	motile cilium
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0050815	molecular_function	phosphoserine residue binding
D	0051219	molecular_function	phosphoprotein binding
D	0051289	biological_process	protein homotetramerization
D	0051495	biological_process	positive regulation of cytoskeleton organization
D	0070207	biological_process	protein homotrimerization
D	0097298	biological_process	regulation of nucleus size
D	1990051	biological_process	activation of protein kinase C activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	ARG60
A	ARG135
A	TYR136
A	SO4305

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 302

Chain	Residue
A	ARG88
A	ARG91
A	GLN92

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 303

Chain	Residue
A	LYS78
A	ARG76
A	GLN77

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 304

Chain	Residue
A	LYS72
A	ARG76

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 305

Chain	Residue
A	LYS128
A	ASP132
A	ASN180
A	SO4301

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 301

Chain	Residue
B	ARG60
B	ARG135
B	TYR136

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 302

Chain	Residue
B	ARG76
B	GLN77
B	LYS78

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 303

Chain	Residue
B	ARG88
B	ARG91
B	GLN92

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 304

Chain	Residue
B	LYS53
B	LYS128
B	ASP132
B	ASN180

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 301

Chain	Residue
C	ARG60
C	ARG135
C	TYR136

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 302

Chain	Residue
C	ARG88
C	ARG91
C	GLN92

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 303

Chain	Residue
C	SER41
C	ASP42
C	ARG45

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 304

Chain	Residue
C	ARG76
C	GLN77
C	LYS78

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 305

Chain	Residue
B	LYS78
C	GLU39
C	ARG116
C	SER117
C	THR118
C	ASN119
C	ALA122

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 301

Chain	Residue
D	ARG60
D	ARG135
D	TYR136

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 302

Chain	Residue
D	ARG88
D	ARG91
D	GLN92

Functional Information from PROSITE/UniProt

site_id	PS00796
Number of Residues	11
Details	1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV

Chain	Residue	Details
A	ARG45-VAL55

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:26551337, ECO:0007744\|PDB:4ZQ0

Chain	Residue	Details
A	ARG135
B	ARG135
C	ARG135
D	ARG135

site_id	SWS_FT_FI2
Number of Residues	8
Details	SITE: Interaction with phosphoserine => ECO:0000269\|PubMed:26551337, ECO:0007744\|PDB:4ZQ0

Chain	Residue	Details
A	LYS53
A	ARG60
B	LYS53
B	ARG60
C	LYS53
C	ARG60
D	LYS53
D	ARG60

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:16368691, ECO:0000269\|PubMed:19733174, ECO:0000269\|PubMed:24147113, ECO:0000269\|PubMed:24658679

Chain	Residue	Details
A	THR214
B	THR214
C	THR214
D	THR214

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: 5-glutamyl polyglycine => ECO:0000269\|PubMed:19733174

Chain	Residue	Details
A	GLU246
B	GLU246
C	GLU246
D	GLU246

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)