5I0I

Crystal structure of myosin X motor domain with 2IQ motifs in pre-powerstroke state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003774	molecular_function	cytoskeletal motor activity
A	0005524	molecular_function	ATP binding
A	0016459	cellular_component	myosin complex
B	0003774	molecular_function	cytoskeletal motor activity
B	0005524	molecular_function	ATP binding
B	0016459	cellular_component	myosin complex
C	0000922	cellular_component	spindle pole
C	0002027	biological_process	regulation of heart rate
C	0005246	molecular_function	calcium channel regulator activity
C	0005509	molecular_function	calcium ion binding
C	0005513	biological_process	detection of calcium ion
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005813	cellular_component	centrosome
C	0005819	cellular_component	spindle
C	0005829	cellular_component	cytosol
C	0005876	cellular_component	spindle microtubule
C	0005886	cellular_component	plasma membrane
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0008076	cellular_component	voltage-gated potassium channel complex
C	0010856	molecular_function	adenylate cyclase activator activity
C	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
C	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
C	0016020	cellular_component	membrane
C	0016240	biological_process	autophagosome membrane docking
C	0019855	molecular_function	calcium channel inhibitor activity
C	0019901	molecular_function	protein kinase binding
C	0021762	biological_process	substantia nigra development
C	0030017	cellular_component	sarcomere
C	0031432	molecular_function	titin binding
C	0031514	cellular_component	motile cilium
C	0031982	cellular_component	vesicle
C	0032465	biological_process	regulation of cytokinesis
C	0032991	cellular_component	protein-containing complex
C	0034704	cellular_component	calcium channel complex
C	0035458	biological_process	cellular response to interferon-beta
C	0043209	cellular_component	myelin sheath
C	0043539	molecular_function	protein serine/threonine kinase activator activity
C	0044305	cellular_component	calyx of Held
C	0044325	molecular_function	transmembrane transporter binding
C	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
C	0046872	molecular_function	metal ion binding
C	0048306	molecular_function	calcium-dependent protein binding
C	0051592	biological_process	response to calcium ion
C	0055117	biological_process	regulation of cardiac muscle contraction
C	0060291	biological_process	long-term synaptic potentiation
C	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
C	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
C	0071346	biological_process	cellular response to type II interferon
C	0072542	molecular_function	protein phosphatase activator activity
C	0097225	cellular_component	sperm midpiece
C	0097720	biological_process	calcineurin-mediated signaling
C	0098901	biological_process	regulation of cardiac muscle cell action potential
C	0099523	cellular_component	presynaptic cytosol
C	0140056	biological_process	organelle localization by membrane tethering
C	0140238	biological_process	presynaptic endocytosis
C	0141110	molecular_function	transporter inhibitor activity
C	1901842	biological_process	negative regulation of high voltage-gated calcium channel activity
C	1901844	biological_process	regulation of cell communication by electrical coupling involved in cardiac conduction
C	1902494	cellular_component	catalytic complex
C	1905913	biological_process	negative regulation of calcium ion export across plasma membrane
C	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering
E	0000922	cellular_component	spindle pole
E	0002027	biological_process	regulation of heart rate
E	0005246	molecular_function	calcium channel regulator activity
E	0005509	molecular_function	calcium ion binding
E	0005513	biological_process	detection of calcium ion
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005813	cellular_component	centrosome
E	0005819	cellular_component	spindle
E	0005829	cellular_component	cytosol
E	0005876	cellular_component	spindle microtubule
E	0005886	cellular_component	plasma membrane
E	0007186	biological_process	G protein-coupled receptor signaling pathway
E	0008076	cellular_component	voltage-gated potassium channel complex
E	0010856	molecular_function	adenylate cyclase activator activity
E	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
E	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
E	0016020	cellular_component	membrane
E	0016240	biological_process	autophagosome membrane docking
E	0019855	molecular_function	calcium channel inhibitor activity
E	0019901	molecular_function	protein kinase binding
E	0021762	biological_process	substantia nigra development
E	0030017	cellular_component	sarcomere
E	0031432	molecular_function	titin binding
E	0031514	cellular_component	motile cilium
E	0031982	cellular_component	vesicle
E	0032465	biological_process	regulation of cytokinesis
E	0032991	cellular_component	protein-containing complex
E	0034704	cellular_component	calcium channel complex
E	0035458	biological_process	cellular response to interferon-beta
E	0043209	cellular_component	myelin sheath
E	0043539	molecular_function	protein serine/threonine kinase activator activity
E	0044305	cellular_component	calyx of Held
E	0044325	molecular_function	transmembrane transporter binding
E	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
E	0046872	molecular_function	metal ion binding
E	0048306	molecular_function	calcium-dependent protein binding
E	0051592	biological_process	response to calcium ion
E	0055117	biological_process	regulation of cardiac muscle contraction
E	0060291	biological_process	long-term synaptic potentiation
E	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
E	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
E	0071346	biological_process	cellular response to type II interferon
E	0072542	molecular_function	protein phosphatase activator activity
E	0097225	cellular_component	sperm midpiece
E	0097720	biological_process	calcineurin-mediated signaling
E	0098901	biological_process	regulation of cardiac muscle cell action potential
E	0099523	cellular_component	presynaptic cytosol
E	0140056	biological_process	organelle localization by membrane tethering
E	0140238	biological_process	presynaptic endocytosis
E	0141110	molecular_function	transporter inhibitor activity
E	1901842	biological_process	negative regulation of high voltage-gated calcium channel activity
E	1901844	biological_process	regulation of cell communication by electrical coupling involved in cardiac conduction
E	1902494	cellular_component	catalytic complex
E	1905913	biological_process	negative regulation of calcium ion export across plasma membrane
E	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering
G	0005509	molecular_function	calcium ion binding
I	0005509	molecular_function	calcium ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MPO A 901

Chain	Residue
A	TYR141
A	TRP145
A	GLN231
A	LYS232
C	HIS107

---

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 902

Chain	Residue
A	HOH1001
A	HOH1006
A	THR164
A	SER219
A	VO4903
A	ADP904

---

site_id	AC3
Number of Residues	11
Details	binding site for residue VO4 A 903

Chain	Residue
A	SER159
A	GLY160
A	LYS163
A	ASN215
A	SER218
A	SER219
A	GLY437
A	MG902
A	ADP904
A	HOH1001
A	HOH1006

---

site_id	AC4
Number of Residues	16
Details	binding site for residue ADP A 904

Chain	Residue
A	ASN104
A	PRO105
A	TYR106
A	GLN107
A	TYR113
A	GLY160
A	ALA161
A	GLY162
A	LYS163
A	THR164
A	GLU165
A	ASN215
A	MG902
A	VO4903
A	HOH1001
A	HOH1006

---

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 A 905

Chain	Residue
A	TYR243
A	LEU244
A	PHE615
A	SER618

---

site_id	AC6
Number of Residues	2
Details	binding site for residue SO4 A 906

Chain	Residue
A	HIS287
A	ARG398

---

site_id	AC7
Number of Residues	4
Details	binding site for residue SO4 A 907

Chain	Residue
A	ARG239
A	TYR243
A	THR625
A	HOH1008

---

site_id	AC8
Number of Residues	6
Details	binding site for residue SO4 A 908

Chain	Residue
A	ALA529
A	ASN530
A	ASN531
A	HIS532
A	TYR534
A	LYS547

---

site_id	AC9
Number of Residues	2
Details	binding site for residue MPO B 901

Chain	Residue
B	GLN231
B	LYS232

---

site_id	AD1
Number of Residues	6
Details	binding site for residue MG B 902

Chain	Residue
B	THR164
B	SER219
B	ADP903
B	VO4904
B	HOH1001
B	HOH1003

---

site_id	AD2
Number of Residues	16
Details	binding site for residue ADP B 903

Chain	Residue
B	ASN104
B	PRO105
B	TYR106
B	GLN107
B	TYR113
B	GLY160
B	ALA161
B	GLY162
B	LYS163
B	THR164
B	GLU165
B	ASN215
B	MG902
B	VO4904
B	HOH1001
B	HOH1003

---

site_id	AD3
Number of Residues	11
Details	binding site for residue VO4 B 904

Chain	Residue
B	SER159
B	GLY160
B	LYS163
B	ASN215
B	SER218
B	SER219
B	GLY437
B	MG902
B	ADP903
B	HOH1001
B	HOH1003

---

site_id	AD4
Number of Residues	4
Details	binding site for residue SO4 B 905

Chain	Residue
B	TYR243
B	LEU244
B	PHE615
B	SER618

---

site_id	AD5
Number of Residues	5
Details	binding site for residue SO4 C 201

Chain	Residue
B	LYS736
C	ASP56
C	ASN60
C	THR62
C	GLU67

---

site_id	AD6
Number of Residues	6
Details	binding site for residue SO4 E 201

Chain	Residue
E	VAL55
E	ASP56
E	ASN60
E	THR62
E	GLU67
A	LYS736

---

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
E	ASP20-LEU32
I	ASP93-LEU105
I	ASP129-PHE141
E	ASP56-PHE68
E	ASP93-LEU105
E	ASP129-PHE141
G	ASP93-LEU105
C	ASP20-LEU32
C	ASP56-PHE68
C	ASP93-LEU105
C	ASP129-PHE141

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1352
Details	Domain: {"description":"Myosin motor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00782","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	42
Details	Domain: {"description":"IQ 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00116","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	44
Details	Region: {"description":"Actin-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00782","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PDB","id":"5I0H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5I0I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	70
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	70
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	70
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	20
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	20
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	15
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	2
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	2
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	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	4
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	4
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	4
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	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	3
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	3
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI20
Number of Residues	4
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

---