6XYR

Structure of the T4Lnano fusion protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000922	cellular_component	spindle pole
A	0002027	biological_process	regulation of heart rate
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
A	0005246	molecular_function	calcium channel regulator activity
A	0005509	molecular_function	calcium ion binding
A	0005513	biological_process	detection of calcium ion
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005819	cellular_component	spindle
A	0005829	cellular_component	cytosol
A	0005876	cellular_component	spindle microtubule
A	0005886	cellular_component	plasma membrane
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0008076	cellular_component	voltage-gated potassium channel complex
A	0009253	biological_process	peptidoglycan catabolic process
A	0010856	molecular_function	adenylate cyclase activator activity
A	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A	0016020	cellular_component	membrane
A	0016240	biological_process	autophagosome membrane docking
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0019855	molecular_function	calcium channel inhibitor activity
A	0019901	molecular_function	protein kinase binding
A	0021762	biological_process	substantia nigra development
A	0030017	cellular_component	sarcomere
A	0030430	cellular_component	host cell cytoplasm
A	0031432	molecular_function	titin binding
A	0031514	cellular_component	motile cilium
A	0031640	biological_process	killing of cells of another organism
A	0031982	cellular_component	vesicle
A	0032465	biological_process	regulation of cytokinesis
A	0032991	cellular_component	protein-containing complex
A	0034704	cellular_component	calcium channel complex
A	0035458	biological_process	cellular response to interferon-beta
A	0042742	biological_process	defense response to bacterium
A	0043209	cellular_component	myelin sheath
A	0043539	molecular_function	protein serine/threonine kinase activator activity
A	0044305	cellular_component	calyx of Held
A	0044325	molecular_function	transmembrane transporter binding
A	0044659	biological_process	viral release from host cell by cytolysis
A	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
A	0046872	molecular_function	metal ion binding
A	0048306	molecular_function	calcium-dependent protein binding
A	0051592	biological_process	response to calcium ion
A	0055117	biological_process	regulation of cardiac muscle contraction
A	0060291	biological_process	long-term synaptic potentiation
A	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
A	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
A	0071346	biological_process	cellular response to type II interferon
A	0072542	molecular_function	protein phosphatase activator activity
A	0097225	cellular_component	sperm midpiece
A	0097720	biological_process	calcineurin-mediated signaling
A	0098901	biological_process	regulation of cardiac muscle cell action potential
A	0099523	cellular_component	presynaptic cytosol
A	0140056	biological_process	organelle localization by membrane tethering
A	0140238	biological_process	presynaptic endocytosis
A	0141110	molecular_function	transporter inhibitor activity
A	1901842	biological_process	negative regulation of high voltage-gated calcium channel activity
A	1901844	biological_process	regulation of cell communication by electrical coupling involved in cardiac conduction
A	1902494	cellular_component	catalytic complex
A	1905913	biological_process	negative regulation of calcium ion export across plasma membrane
A	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 401

Chain	Residue
A	ASP233
A	ASP235
A	ASP237
A	THR239
A	GLU244
A	HOH533

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 402

Chain	Residue
A	THR275
A	GLU280
A	HOH537
A	ASP269
A	ASP271
A	ASN273

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 403

Chain	Residue
A	ASP342
A	ASP344
A	ASP346
A	GLN348
A	GLU353
A	HOH559

---

site_id	AC4
Number of Residues	6
Details	binding site for residue CA A 404

Chain	Residue
A	ASP306
A	ASP308
A	ASN310
A	TYR312
A	GLU317
A	HOH605

---

site_id	AC5
Number of Residues	4
Details	binding site for residue CA A 405

Chain	Residue
A	PHE149
A	SER152
A	ASN167
A	HOH611

---

site_id	AC6
Number of Residues	3
Details	binding site for residue GOL A 406

Chain	Residue
A	TYR123
A	ALA128
A	HOH590

---

site_id	AC7
Number of Residues	4
Details	binding site for residue GOL A 407

Chain	Residue
A	GLY148
A	SER171
A	HOH504
A	HOH545

---

site_id	AC8
Number of Residues	3
Details	binding site for residue GOL A 408

Chain	Residue
A	ASP45
A	GLU46
A	GOL410

---

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL A 409

Chain	Residue
A	THR177
A	PRO178
A	ASN179
A	ARG180
A	GOL410
A	HOH544

---

site_id	AD1
Number of Residues	5
Details	binding site for residue GOL A 410

Chain	Residue
A	ILE44
A	ASP45
A	ARG183
A	GOL408
A	GOL409

---

site_id	AD2
Number of Residues	4
Details	binding site for residue CL A 411

Chain	Residue
A	ASP82
A	ASN90
A	ARG154
A	ARG160

---

site_id	AD3
Number of Residues	4
Details	binding site for residue CL A 412

Chain	Residue
A	ASP127
A	LYS159
A	ASN273
A	HOH630

---

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL

Chain	Residue	Details
A	ASP233-LEU245
A	ASP269-PHE281
A	ASP306-LEU318
A	ASP342-PHE354

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	35
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	35
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	35
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25441029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V0C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29724949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI20
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU46	proton shuttle (general acid/base)
A	ASP55	covalent catalysis

---