1VCP: Semliki forest virus capsid protein

Semliki forest virus capsid protein (crystal form I). Determined by X-ray diffraction at 3.0 Å resolution. Released 7 Dec 1996.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Semliki forest virus
Chains: 3
Atoms: 3,429
Mol. weight: 49.36 kDa
Ligands: HG
Released: 7 Dec 1996

Explore 1VCP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1VCP contains 8 α-helices and 52 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: 2 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	120-125	6	1
β-strand	128-134	7	1
β-strand	136	1	2
β-strand	139-140	2	3
β-strand	141	1	1
β-strand	143	1	4
β-strand	149-150	2	1
α-helix	153-156	4
β-strand	161-163	3	4
β-strand	168-170	3	4
β-strand	171-172	2	3
α-helix	175-180	6
β-strand	182	1	2
β-strand	184	1	5
β-strand	191-195	5	5
β-strand	198-203	6	5
β-strand	206-210	5	5
β-strand	222-224	3	5
β-strand	230-239	10	5
β-strand	243-251	9	5
β-strand	256-259	4	5
β-strand	265-266	2	5

Chain B: 3 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	120-125	6	6
β-strand	128-136	9	6
β-strand	139-143	5	6
β-strand	149-150	2	6
α-helix	153-156	4
β-strand	160-163	4	6
β-strand	168-172	5	6
α-helix	173-174	2
α-helix	175-180	6
β-strand	182	1	6
β-strand	184	1	7
β-strand	191-195	5	7
β-strand	198-202	5	7
β-strand	207-210	4	7
β-strand	222-224	3	7
β-strand	230-239	10	7
β-strand	243-252	10	7
β-strand	255-259	5	7
β-strand	264-265	2	7

Chain C: 3 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	120-124	5	8
β-strand	129-136	8	8
β-strand	139-143	5	8
β-strand	149-150	2	8
α-helix	153-156	4
β-strand	159-160	2	6
β-strand	161-163	3	8
β-strand	168-172	5	8
α-helix	173-174	2
α-helix	175-180	6
β-strand	182	1	8
β-strand	191-195	5	9
β-strand	198-203	6	9
β-strand	206-210	5	9
β-strand	222-224	3	9
β-strand	230-240	11	9
β-strand	243-252	10	9
β-strand	255-259	5	9
β-strand	265	1	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Semliki forest virus capsid protein	A, B, C	protein	149	Semliki forest virus	P03315 (AlphaFold model)

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

>1VCP_1 SEMLIKI FOREST VIRUS CAPSID PROTEIN (chains A, B, C)
CIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMR
SDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGA
NEGSRTALSVVTWNKDMVTRVTPEGSEEW

Ligands and cofactors

ID	Name	Formula	Copies
HG	Mercury (II) ion	Hg	3

Primary citation

Structure of Semliki Forest virus core protein. Choi, H.K., Lu, G., Lee, S. et al. Proteins (1997) 27:345-359. DOI 10.1002/(SICI)1097-0134(199703)27:3<345::AID-PROT3>3.0.CO;2-C · PubMed

Other PDB entries of the same protein (UniProt P03315 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2V33 1.55 Å, High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki…
1I9W 3.0 Å, Crystal structure of the fusion glycoprotein E1 from semliki forest virus
2ALA 3.0 Å, Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric…
8IHP 3.0 Å, Structure of Semliki Forest virus VLP in complex with the receptor VLDLR-LA3
8YVY 3.02 Å, Semliki Forest virus virion
1VCQ 3.1 Å, Semliki forest virus capsid protein (crystal form II)
1RER 3.2 Å, Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus.
8YW1 3.44 Å, Semliki Forest virus viron in complex with VLDLR
8YVZ 3.45 Å, Semliki Forest virus viron
8X0K 3.5 Å, Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(2-fold)
8X0L 3.5 Å, Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(3-fold)
8X0M 3.5 Å, Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold)

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