4ZRK: Merlin-FERM and Lats1 complex

Merlin-FERM and Lats1 complex. Determined by X-ray diffraction at 2.32 Å resolution. Released 17 Jun 2015.

Method: X-ray diffraction
Resolution: 2.32 Å
Organisms: Mus musculus, Homo sapiens
Chains: 8
Atoms: 10,303
Mol. weight: 166.6 kDa
Released: 17 Jun 2015

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

Secondary structure: helices and β-sheets

4ZRK contains 57 α-helices and 58 β-strands across 8 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: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	21-27	7	1
β-strand	32-38	7	1
β-strand	42	1	2
α-helix	43-54	12
α-helix	59-61	3
β-strand	62-67	6	1
β-strand	72-74	3	1
β-strand	80	1	2
α-helix	81-83	3
β-strand	92-98	7	1
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
α-helix	181-193	13
α-helix	200-211	12
β-strand	220-226	7	3
β-strand	231-236	6	3
β-strand	240-244	5	3
β-strand	254-257	4	3
α-helix	258-260	3
β-strand	261-267	7	3
β-strand	270-275	6	3
α-helix	281-282	2
β-strand	283-286	4	3
α-helix	290-309	20

Chain B: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	21-27	7	4
β-strand	32-38	7	4
β-strand	42	1	5
α-helix	43-54	12
α-helix	59-61	3
β-strand	62-68	7	4
β-strand	71-74	4	4
β-strand	80	1	5
α-helix	81-83	3
β-strand	92-98	7	4
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
α-helix	181-192	12
α-helix	193-195	3
α-helix	200-211	12
β-strand	220-225	6	6
β-strand	231-236	6	6
β-strand	240-244	5	6
β-strand	254-257	4	6
α-helix	258-260	3
β-strand	261-267	7	6
β-strand	270-275	6	6
β-strand	283-286	4	6
α-helix	290-309	20

Chain C: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	21-27	7	7
β-strand	32-38	7	7
β-strand	42	1	8
α-helix	43-54	12
α-helix	59-61	3
β-strand	62-68	7	7
β-strand	71-74	4	7
β-strand	80	1	8
α-helix	81-83	3
β-strand	92-98	7	7
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
β-strand	177	1	9
α-helix	181-192	12
α-helix	193-195	3
α-helix	200-211	12
β-strand	220-226	7	10
β-strand	231-236	6	10
β-strand	240-244	5	10
β-strand	254-257	4	10
α-helix	258-260	3
β-strand	261-267	7	10
β-strand	270-275	6	10
α-helix	281-282	2
β-strand	283-286	4	10
α-helix	290-309	20

Chain D: 13 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	21-27	7	11
β-strand	32-38	7	11
β-strand	42	1	12
α-helix	43-54	12
α-helix	59-61	3
β-strand	62-68	7	11
β-strand	71-74	4	11
β-strand	80	1	12
α-helix	81-83	3
β-strand	92-98	7	11
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
α-helix	181-192	12
α-helix	193-195	3
α-helix	200-211	12
β-strand	220-226	7	13
β-strand	231-237	7	13
β-strand	240-244	5	13
β-strand	254-257	4	13
α-helix	258-260	3
β-strand	261-267	7	13
β-strand	270-275	6	13
α-helix	281-282	2
β-strand	283-286	4	13
α-helix	290-310	21

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	74-85	12

Chains F and H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	74-85	12
α-helix	86-88	3

Chain G: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	74-85	12
α-helix	86-88	3
β-strand	89	1	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Merlin	A, B, C, D	protein	324	Mus musculus	P46662 (AlphaFold model)
Serine/threonine-protein kinase LATS1	E, F, G, H	protein	32	Homo sapiens	O95835 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4ZRK_1 Merlin (chains A, B, C, D)
GPGSMAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGL
RETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQH
LFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINL
YQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGV
DALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLI
LQLCIGNHDLFMRRRKADSLEVQQ

Sequence of entity 2 (E, F, G, H), FASTA

>4ZRK_2 Serine/threonine-protein kinase LATS1 (chains E, F, G, H)
PKFGTHHKALQEIRNSLLPFANETNSSRSTSE

Primary citation

Angiomotin binding-induced activation of Merlin/NF2 in the Hippo pathway. Li, Y., Zhou, H., Li, F. et al. Cell Res (2015) 25:801-817. DOI 10.1038/cr.2015.69 · PubMed

Other PDB entries of the same protein (UniProt P46662 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3WA0 2.31 Å, Crystal structure of merlin complexed with DCAF1/VprBP
4P7I 2.6 Å, Crystal structure of the Merlin FERM/DCAF1 complex
1ISN 2.9 Å, Crystal structure of merlin FERM domain

Browse structure collections

About this viewer

MolViewer shows 4ZRK directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.