4N7G

Crystal structure of 14-3-3zeta in complex with a peptide derived from ExoS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0001525	biological_process	angiogenesis
A	0003016	biological_process	respiratory system process
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005925	cellular_component	focal adhesion
A	0006468	biological_process	protein phosphorylation
A	0007165	biological_process	signal transduction
A	0008039	biological_process	synaptic target recognition
A	0008104	biological_process	intracellular protein localization
A	0019901	molecular_function	protein kinase binding
A	0019903	molecular_function	protein phosphatase binding
A	0019904	molecular_function	protein domain specific binding
A	0030324	biological_process	lung development
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0031647	biological_process	regulation of protein stability
A	0031982	cellular_component	vesicle
A	0035148	biological_process	tube formation
A	0042149	biological_process	cellular response to glucose starvation
A	0042470	cellular_component	melanosome
A	0042802	molecular_function	identical protein binding
A	0043066	biological_process	negative regulation of apoptotic process
A	0044325	molecular_function	transmembrane transporter binding
A	0045296	molecular_function	cadherin binding
A	0045824	biological_process	negative regulation of innate immune response
A	0050815	molecular_function	phosphoserine residue binding
A	0051683	biological_process	establishment of Golgi localization
A	0070062	cellular_component	extracellular exosome
A	0070372	biological_process	regulation of ERK1 and ERK2 cascade
A	0072562	cellular_component	blood microparticle
A	0090128	biological_process	regulation of synapse maturation
A	0090168	biological_process	Golgi reassembly
A	0098686	cellular_component	hippocampal mossy fiber to CA3 synapse
A	0098978	cellular_component	glutamatergic synapse
A	0140297	molecular_function	DNA-binding transcription factor binding
A	0140311	molecular_function	protein sequestering activity
A	1900181	biological_process	negative regulation of protein localization to nucleus
A	1904262	biological_process	negative regulation of TORC1 signaling

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE P6G A 301

Chain	Residue
A	GLU5
A	LYS9
A	MET78
A	GLU81
A	THR88
A	ALA201

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE P6G A 302

Chain	Residue
A	ASP136
A	ILE155
A	GLU159
A	SER110
A	LYS115
A	GLY135

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE P6G A 303

Chain	Residue
A	SER99
A	GLU102
A	LEU119
A	LYS122
A	GLN144
A	ALA148
A	GLU151

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE P6G A 304

Chain	Residue
A	GLU17
A	GLU17
A	TYR19
A	ASN50
A	ALA54
A	SER57
A	SER58
A	HOH407

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE P6G A 305

Chain	Residue
A	GLN32
A	GLY33
A	LYS103
A	PRO107
A	ASN108
A	HOH452

---

site_id	AC6
Number of Residues	24
Details	BINDING SITE FOR CHAIN B OF EXOENZYME S

Chain	Residue
A	ARG41
A	ASN42
A	SER45
A	VAL46
A	LYS49
A	PHE117
A	LYS120
A	TYR128
A	PRO165
A	GLY169
A	LEU172
A	ASN173
A	ASP213
A	ILE217
A	ASN224
A	HOH405
B	HOH501
B	HOH502
B	HOH503
B	HOH504
B	HOH505
B	HOH506
B	HOH507
B	HOH508

---

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	ARG41-VAL51

---

site_id	PS00797
Number of Residues	20
Details	1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS

Chain	Residue	Details
A	TYR211-SER230

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Site: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"source":"UniProtKB","id":"P63103","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Potts A.","Barblan J.","Claeys D.","Quadroni M."]}},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKA and PKB/AKT1","evidences":[{"source":"PubMed","id":"11956222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12865427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15883165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16376338","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by MAPK8","evidences":[{"source":"PubMed","id":"15071501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15696159","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63102","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---