4ANJ: PDB entry 4ANJ

MYOSIN VI (MDinsert2-GFP fusion) PRE-POWERSTROKE STATE (MG.ADP.AlF4). Determined by X-ray diffraction at 2.6 Å resolution. Released 17 Oct 2012.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: SUS SCROFA, AEQUOREA VICTORIA, DROSOPHILA MELANOGASTER
Chains: 2
Atoms: 8,845
Mol. weight: 137.63 kDa
Ligands: ADP, MG, ALF, CA
Released: 17 Oct 2012

Explore 4ANJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ANJ contains 58 α-helices and 48 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 50 helices, 46 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	1
β-strand	15-24	10	1
β-strand	28-33	6	1
β-strand	41-44	4	1
α-helix	45-47	3
β-strand	49-50	2	1
β-strand	61	1	2
α-helix	62-64	3
α-helix	70-82	13
β-strand	87-90	4	2
β-strand	93-97	5	2
α-helix	109-115	7
α-helix	118-119	2
β-strand	120	1	3
β-strand	123	1	3
α-helix	127-141	15
β-strand	145-150	6	2
α-helix	157-172	16
α-helix	181-184	4
α-helix	186-193	8
β-strand	194-195	2	4
β-strand	203-204	2	4
β-strand	207-214	8	2
β-strand	220-228	9	2
α-helix	233-235	3
β-strand	245	1	4
α-helix	246-254	9
α-helix	257-263	7
α-helix	268-270	3
α-helix	272-275	4
α-helix	280-281	2
β-strand	282	1	5
α-helix	285-288	4
α-helix	293-295	3
α-helix	298-303	6
β-strand	306	1	5
α-helix	313-327	15
α-helix	331-348	18
β-strand	352-353	2	6
β-strand	363-364	2	6
α-helix	366-368	3
α-helix	369-378	10
α-helix	383-391	9
β-strand	392-393	2	7
β-strand	409-410	2	7
α-helix	413-440	28
β-strand	450-456	7	2
α-helix	457-459	3
α-helix	468-484	17
α-helix	485-490	6
α-helix	491-498	8
α-helix	503-505	3
α-helix	512-519	8
α-helix	525-534	10
α-helix	540-549	10
β-strand	557-558	2	8
α-helix	560-562	3
β-strand	576-581	6	8
β-strand	584-589	6	8
α-helix	593-597	5
β-strand	598	1	9
α-helix	603-610	8
α-helix	615-619	5
β-strand	642	1	9
α-helix	643-659	17
β-strand	662-669	8	2
α-helix	682-692	11
α-helix	694-700	7
β-strand	707-710	4	10
α-helix	711-719	9
α-helix	726-728	3
α-helix	731-741	11
α-helix	746-748	3
β-strand	749-751	3	10
β-strand	755-758	4	10
α-helix	763-770	8
α-helix	774-1006	49
β-strand	1012-1022	11	11
β-strand	1025-1036	12	11
β-strand	1041-1048	8	11
α-helix	1057-1060	4
α-helix	1069-1071	3
β-strand	1073	1	11
α-helix	1076-1081	6
α-helix	1083-1086	4
β-strand	1092-1100	9	11
β-strand	1105-1115	11	11
β-strand	1118-1128	11	11
β-strand	1141	1	12
β-strand	1148-1155	8	11
β-strand	1160-1170	11	11
β-strand	1171	1	12
β-strand	1176-1187	12	11
α-helix	1194-1197	4
β-strand	1199-1208	10	11
β-strand	1217-1227	11	11

Chain B: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	6-16	11
α-helix	32-38	7
α-helix	46-52	7
α-helix	65-71	7
α-helix	81-92	12
β-strand	100	1	13
α-helix	102-109	8
α-helix	118-128	11
β-strand	136	1	13
α-helix	138-145	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Unconventional myosin-VI, green fluorescent protein	A	protein	1052	SUS SCROFA, AEQUOREA VICTORIA	P42212 (AlphaFold model), Q29122 (AlphaFold model)
Calmodulin	B	protein	149	DROSOPHILA MELANOGASTER	P62152 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4ANJ_1 UNCONVENTIONAL MYOSIN-VI, GREEN FLUORESCENT PROTEIN (chains A)
MEDGKPVWAPHPTDGFQVGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVE
DNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSETIKSYQGKSL
GTMPPHVFAIADKAFRDMKVLKLSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDD
RIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGK
EERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEY
LKAGSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSG
GCNLKNKSTQALEYCAELLGLDQDDLRVSLTTRVMLTTAGGAKGTVIKVPLKVEQANNAR
DALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKL
QQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEARLVGILDILDEENRLPQPSD
QHFTSAVHQKHKDHFRLSIPRKSKLAIHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDA
LHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRS
TGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKK
YMPDKLARLDPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAEL
VKRVNHWLICSRWKKVQWCSLSVIKLKNKIKYRAEAVSKGEELFTGVVPILVELDGDVNG
HKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFXVQCFARYPDHMRQHDFFKS
AMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYN
SHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSYQSA
LSKDPNEKRDHMVLLEFVTAAGITHGMDELYK

Sequence of entity 2 (B), FASTA

>4ANJ_2 CALMODULIN (chains B)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVTMMTSK

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
MG	Magnesium ion	Mg	1
ALF	Tetrafluoroaluminate ion	Al F4	1
CA	Calcium ion	Ca	3

Primary citation

Processive Steps in the Reverse Direction Require Uncoupling of the Lead Head Lever Arm of Myosin Vi. Menetrey, J., Isabet, T., Ropars, V. et al. Mol Cell (2012) 48:75. DOI 10.1016/J.MOLCEL.2012.07.034 · PubMed

Other PDB entries of the same protein (UniProt P42212 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6L27 0.77 Å, X-ray crystal structure of the mutant green fluorescent protein
6JGJ 0.78 Å, Crystal structure of the F99S/M153T/V163A/E222Q variant of GFP at 0.78 A
6KL0 0.8 Å, Crystal structure of the S65T/F99S/M153T/V163A variant of perdeuterated GFP at pD 7.0
6JGI 0.85 Å, Crystal structure of the S65T/F99S/M153T/V163A variant of GFP at 0.85 A
6KL1 0.85 Å, Crystal structure of the S65T/F99S/M153T/V163A variant of non-deuterated GFP at pD 8.5
2WUR 0.9 Å, Atomic resolution structure of GFP measured on a rotating anode
6KKZ 0.9 Å, Crystal structure of the S65T/F99S/M153T/V163A variant of perdeuterated GFP at pD 8.5
6JGH 0.94 Å, Crystal structure of the F99S/M153T/V163A/T203I variant of GFP at 0.94 A
4AS8 1.02 Å, X-ray structure of the cyan fluorescent protein Cerulean cryoprotected with ethylene…
5OXC 1.02 Å, Structure of Cerulean Fluorescent Protein at 1.02 Angstrom resolution
7PCA 1.05 Å, Functional and structural characterization of redox sensitive superfolder green…
4GF6 1.1 Å, crystal structure of GFP with cuprum bound at the Incorporated metal Chelating Amino…

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