Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4DBP

Myosin VI nucleotide-free (MDINSERT2) D179Y crystal structure

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
A	0051015	molecular_function	actin filament binding
C	0000226	biological_process	microtubule cytoskeleton organization
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005813	cellular_component	centrosome
C	0005814	cellular_component	centriole
C	0005819	cellular_component	spindle
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005938	cellular_component	cell cortex
C	0007099	biological_process	centriole replication
C	0007605	biological_process	sensory perception of sound
C	0007608	biological_process	sensory perception of smell
C	0016028	cellular_component	rhabdomere
C	0016056	biological_process	G protein-coupled opsin signaling pathway
C	0016059	biological_process	negative regulation of opsin-mediated signaling pathway
C	0016060	biological_process	negative regulation of phospholipase C-activating phototransduction signaling pathway
C	0016247	molecular_function	channel regulator activity
C	0030048	biological_process	actin filament-based movement
C	0030234	molecular_function	enzyme regulator activity
C	0030496	cellular_component	midbody
C	0031475	cellular_component	myosin V complex
C	0031476	cellular_component	myosin VI complex
C	0031477	cellular_component	myosin VII complex
C	0031489	molecular_function	myosin V binding
C	0032036	molecular_function	myosin heavy chain binding
C	0042052	biological_process	rhabdomere development
C	0046716	biological_process	muscle cell cellular homeostasis
C	0046872	molecular_function	metal ion binding
C	0048102	biological_process	autophagic cell death
C	0050911	biological_process	detection of chemical stimulus involved in sensory perception of smell
C	0051383	biological_process	kinetochore organization
C	0070855	molecular_function	myosin VI head/neck binding
C	0071361	biological_process	cellular response to ethanol
C	0072499	biological_process	photoreceptor cell axon guidance
C	0072686	cellular_component	mitotic spindle
C	0097431	cellular_component	mitotic spindle pole

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TBU A 901

Chain	Residue
A	ARG205
A	PHE206
A	LEU229
A	HOH1528

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TBU A 902

Chain	Residue
A	THR158
A	LEU165
A	ASN186
A	LYS208

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 903

Chain	Residue
A	LYS720
A	ASP767
A	LYS771
A	MET717

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 904

Chain	Residue
A	ASN284
A	ASP288
A	GLY304
A	SER305
A	HOH1454

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 905

Chain	Residue
A	ARG487
A	HOH1482
A	HOH1599

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 906

Chain	Residue
A	TYR100
A	LYS670
A	LEU673
A	HOH1114
A	HOH1511
A	HOH1547

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 907

Chain	Residue
A	LYS550
A	HIS551
A	ASP553
A	HIS554

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 908

Chain	Residue
A	VAL7
A	PRO50
A	HOH1345
A	HOH1584

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 909

Chain	Residue
A	LYS142
A	LEU143
A	SER144
A	SER449
A	HOH1406

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 910

Chain	Residue
A	ARG556
A	HIS581
A	PHE582

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 911

Chain	Residue
A	PRO50
A	LEU68
A	ASN69
A	GLY761
A	HOH1588

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 912

Chain	Residue
A	ALA253
A	GLY254
A	ALA255
A	GLN290
A	ILE291
A	LEU292
A	ARG295
A	HIS314

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 913

Chain	Residue
A	ASN275
A	THR279
A	GLU299
A	HOH1034

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 914

Chain	Residue
A	THR197
A	VAL198
A	ARG205
A	GLU242
A	GLU461
A	PHE463
A	HOH1045

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 915

Chain	Residue
A	LYS232
A	SER233
A	HOH1528

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 916

Chain	Residue
A	GLU505
A	HIS507

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 917

Chain	Residue
A	GLY173
A	THR174
A	GLY175
A	GLN176
A	ASP177
A	ILE178
A	VAL220

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 918

Chain	Residue
A	GLU231
A	SER233
A	ARG234
A	VAL237
A	HOH1216

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 919

Chain	Residue
A	LYS498
C	PHE65
C	PRO66

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 920

Chain	Residue
A	PHE49
A	ASN69
A	GLU70
A	ASP699
A	GLN702

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IPA A 921

Chain	Residue
A	ASN477
A	GLN481
A	ARG667
A	SER692
A	HOH1239
A	HOH1583

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 201

Chain	Residue
C	ASP24
C	THR26
C	GLU31
C	HOH303
C	ASP20
C	ASP22

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 202

Chain	Residue
C	ASP56
C	ASP58
C	ASN60
C	THR62
C	GLU67

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 203

Chain	Residue
C	ASP93
C	ASP95
C	ASN97
C	PHE99
C	GLU104

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 204

Chain	Residue
C	ASP129
C	ASP131
C	ASP133
C	GLN135
C	GLU140

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
C	ASP20-LEU32
C	ASP56-PHE68
C	ASP93-LEU105
C	ASP129-PHE141

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	44
Details	Region: {"description":"Responsible for slow ATPase activity","evidences":[{"source":"PubMed","id":"15944696","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	7
Details	Region: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	28
Details	Region: {"description":"Required for binding calmodulin","evidences":[{"source":"PubMed","id":"15037754","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9UM54","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"12682054","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64331","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
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_FI14
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_FI15
Number of Residues	19
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Site: {"description":"Not N6-methylated"}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"17610210","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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