4V0P: MAGE homology domain of human MAGE-A3

Crystal structure of the MAGE homology domain of human MAGE-A3. Determined by X-ray diffraction at 2.07 Å resolution. Released 1 Oct 2014.

Method
X-ray diffraction
Resolution
2.07 Å
Organism
HOMO SAPIENS
Chains
1
Atoms
1,764
Mol. weight
24.12 kDa
Released
1 Oct 2014

Explore 4V0P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4V0P contains 14 α-helices and 6 β-strands across 1 chain. 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: 14 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix103-12624
β-strand130-13121
α-helix132-1387
α-helix141-1466
α-helix147-16216
β-strand164-17071
β-strand175-18061
α-helix181-1833
α-helix199-21214
β-strand216-21722
α-helix218-2258
α-helix229-2313
α-helix242-25211
β-strand256-26052
α-helix2611
β-strand269-27352
α-helix275-2806
α-helix283-29210
α-helix301-3033
α-helix304-3063

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Melanoma-associated antigen 3Aprotein213HOMO SAPIENSP43357 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4V0P_1 MELANOMA-ASSOCIATED ANTIGEN 3 (chains A)
SMEFQAALSRKVAELVHFLLLKYRAREPVTKAEMLGSVVGNWQYFFPVIFSKASSSLQLV
FGIELMEVDPIGHLYIFATCLGLSYDGLLGDNQIMPKAGLLIIVLAIIAREGDCAPEEKI
WEELSVLEVFEGREDSILGDPKKLLTQHFVQENYLEYRQVPGSDPACYEFLWGPRALVET
SYVKVLHHMVKISGGPHISYPPLHEWVLREGEE

Primary citation

Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding. Newman, J.A., Cooper, C.D.O., Roos, A.K. et al. PLoS One (2016) 11:48762. DOI 10.1371/JOURNAL.PONE.0148762 · PubMed

Other PDB entries of the same protein (UniProt P43357 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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