2MSC: Apolipoprotein A-I

NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc. Determined by solution NMR. Released 3 Jun 2015.

Method: Solution NMR
Organism: Homo sapiens
Chains: 3
Atoms: 9,072
Mol. weight: 131.18 kDa
Ligands: PCW, 17F, GDP, MG
Released: 3 Jun 2015

Explore 2MSC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2MSC contains 12 α-helices and 8 β-strands across 3 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: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	202-247	46
α-helix	248-252	5
α-helix	254-309	56
α-helix	313-361	49
α-helix	366-393	28

Chain B: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	1
α-helix	16-24	9
β-strand	39-46	8	1
β-strand	49-57	9	1
α-helix	66-74	9
β-strand	77-83	7	1
α-helix	87-104	18
β-strand	111-116	6	1
α-helix	127-137	11
β-strand	141-143	3	1
β-strand	145	1	2
β-strand	150	1	2
α-helix	152-172	21

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	400-418	19
α-helix	421-591	171

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apolipoprotein A-I	A, C	protein	200	Homo sapiens	P02647 (AlphaFold model)
GTPase KRas	B	protein	187	Homo sapiens	P01116 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2MSC_1 Apolipoprotein A-I (chains A, C)
GPLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYL
DDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRT
HLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPV
LESFKVSFLSALEEYTKKLN

Sequence of entity 2 (B), FASTA

>2MSC_2 GTPase KRas (chains B)
GSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDT
AGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKC
DLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEKMSKDGKKKK
KKSKTKC

Ligands and cofactors

ID	Name	Formula	Copies
PCW	1,2-dioleoyl-sn-glycero-3-phosphocholine	C44 H85 N O8 P	64
17F	O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L…	C42 H78 N O10 P	16
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
MG	Magnesium ion	Mg	1

Primary citation

Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Mazhab-Jafari, M.T., Marshall, C.B., Smith, M.J. et al. Proc Natl Acad Sci U S A (2015) 112:6625-6630. DOI 10.1073/pnas.1419895112 · PubMed

Other PDB entries of the same protein (UniProt P02647 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7KJR 2.08 Å, Cryo-EM structure of SARS-CoV-2 ORF3a
9PVY 2.15 Å, Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I L90P…
3R2P 2.2 Å, 2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals…
9PVZ 2.3 Å, Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I R173P…
8VXJ 2.7 Å, The crystal structure of human apolipoprotein A-I in complex with Fab 55201
9PW3 2.73 Å, Cryo-EM structure of renal amyloid fibril from a variant apolipoprotein A-I R173P…
8EQS 3.1 Å, Structure of SARS-CoV-1 Orf3a in late endosome/lysosome-like environment, MSP1D1 nanodisc
1AV1 4.0 Å, Crystal structure of human apolipoprotein a-I
4V6M 7.1 Å, Structure of the ribosome-SecYE complex in the membrane environment
9MXZ 9.8 Å, Lecithin:Cholesterol Acyltransferase Bound to Apolipoprotein A-I dimer in HDL
1GW3 The helix-hinge-helix structural motif in human apolipoprotein a-I determined by NMR…
1GW4 The helix-hinge-helix structural motif in human apolipoprotein a-I determined by NMR…

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