1MA3: Sir2 enzyme

Structure of a Sir2 enzyme bound to an acetylated p53 peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Oct 2002.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Archaeoglobus fulgidus
Chains: 2
Atoms: 2,123
Mol. weight: 30.94 kDa
Ligands: ZN
Released: 16 Oct 2002

Explore 1MA3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MA3 contains 18 α-helices and 15 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: 18 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	2-14	13
β-strand	18-22	5	1
α-helix	24-26	3
α-helix	47-50	4
β-strand	52	1	2
α-helix	53-56	4
α-helix	60-69	10
α-helix	71-74	4
α-helix	80-90	11
β-strand	94-99	6	1
α-helix	105-109	5
β-strand	114-116	3	1
β-strand	119-126	8	3
β-strand	132-134	3	3
α-helix	135-137	3
α-helix	139-143	5
α-helix	146-148	3
β-strand	158-162	5	3
α-helix	163-164	2
β-strand	165	1	2
β-strand	168	1	4
α-helix	169-170	2
α-helix	171-183	13
β-strand	186-190	5	1
β-strand	196-197	2	5
α-helix	199-201	3
α-helix	202-209	8
β-strand	212-217	6	1
α-helix	224-226	3
β-strand	229-232	4	1
α-helix	235-249	15

Chain B: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	10	1	4
β-strand	12-13	2	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional regulatory protein, Sir2 family	A	protein	253	Archaeoglobus fulgidus	O30124 (AlphaFold model)
Cellular tumor antigen p53	B	protein	18		P04637 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1MA3_1 Transcriptional regulatory protein, Sir2 family (chains A)
MEDEIRKAAEILAKSKHAVVFTGAGISAESGIPTFRGEDGLWRKYDPEEVASISGFKRNP
RAFWEFSMEMKDKLFAEPNPAHYAIAELERMGIVKAVITQNIDMLHQRAGSRRVLELHGS
MDKLDCLDCHETYDWSEFVEDFNKGEIPRCRKCGSYYVKPRVVLFGEPLPQRTLFEAIEE
AKHCDAFMVVGSSLVVYPAAELPYIAKKAGAKMIIVNAEPTMADPIFDVKIIGKAGEVLP
KIVEEVKRLRSEK

Sequence of entity 2 (B), FASTA

>1MA3_2 Cellular tumor antigen p53 (chains B)
KKGQSTSRHKKLMFKTEG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Water and common crystallization additives (MES) are not listed.

Primary citation

Structure of a Sir2 enzyme bound to an acetylated p53 peptide. Avalos, J.L., Celic, I., Muhammad, S. et al. Mol Cell (2002) 10:523-535. DOI 10.1016/S1097-2765(02)00628-7 · PubMed

Other PDB entries of the same protein (UniProt O30124 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4TWJ 1.65 Å, The structure of Sir2Af2 bound to a myristoylated histone peptide
1S7G 2.3 Å, Structural Basis for the Mechanism and Regulation of Sir2 Enzymes
1YC2 2.4 Å, Sir2Af2-NAD-ADPribose-nicotinamide

Browse structure collections

About this viewer

MolViewer shows 1MA3 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.