6CDS: Merlin

Human neurofibromin 2/merlin/schwannomin residues 1-339 in complex with PIP2. Determined by X-ray diffraction at 2.62 Å resolution. Released 18 Jul 2018.

Method: X-ray diffraction
Resolution: 2.62 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,713
Mol. weight: 82.35 kDa
Ligands: PIO, PO4
Released: 18 Jul 2018

Explore 6CDS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CDS contains 26 α-helices and 30 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: 13 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	62-68	7	1
β-strand	71-74	4	1
α-helix	75-76	2
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	171-177	7
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	261-266	6	3
β-strand	270-275	6	3
α-helix	281-282	2
β-strand	283-286	4	3
α-helix	290-337	48

Chain B: 13 helices, 16 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
α-helix	75-76	2
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	183-193	11
α-helix	200-211	12
β-strand	220-226	7	6
β-strand	231-237	7	6
β-strand	240-244	5	6
β-strand	245	1	7
β-strand	248	1	7
β-strand	254-257	4	6
α-helix	258-260	3
β-strand	261-266	6	6
β-strand	270-275	6	6
α-helix	281-282	2
β-strand	283-286	4	6
α-helix	290-337	48

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Merlin	A, B	protein	339	Homo sapiens	P35240 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6CDS_1 Merlin (chains A, B)
MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETW
FFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFL
QVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMT
PEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALG
LHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLC
IENHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRL

Ligands and cofactors

ID	Name	Formula	Copies
PIO	[(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-d…	C25 H49 O19 P3	2
PO4	Phosphate ion	O4 P	2

Water and common crystallization additives (GOL, PEG) are not listed.

Primary citation

Lipid binding promotes the open conformation and tumor-suppressive activity of neurofibromin 2. Chinthalapudi, K., Mandati, V., Zheng, J. et al. Nat Commun (2018) 9:1338-1338. DOI 10.1038/s41467-018-03648-4 · PubMed

Other PDB entries of the same protein (UniProt P35240 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7LWH 1.61 Å, Human neurofibromin 2/merlin residues 1-339 in complex with LATS1
1H4R 1.8 Å, Crystal Structure of the FERM domain of Merlin, the Neurofibromatosis 2 Tumor Suppressor…
4ZRJ 2.3 Å, Structure of Merlin-FERM and CTD
3U8Z 2.64 Å, human merlin FERM domain
4ZRI 2.7 Å, Crystal structure of Merlin-FERM and Lats2

Browse structure collections

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