4IQY: O-acetyl-ADP-ribose deacetylase MACROD2

Name: PDB 4IQY: Crystal structure of the human protein-proximal ADP-ribosyl-hydrolase MacroD2
Published: 2013-03-06
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: hydrolase

Crystal structure of the human protein-proximal ADP-ribosyl-hydrolase MacroD2. Determined by X-ray diffraction at 1.55 Å resolution. Released 6 Mar 2013.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,079
Mol. weight: 55.31 kDa
Ligands: MG, AR6
Released: 6 Mar 2013

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

Secondary structure: helices and β-sheets

4IQY contains 25 α-helices and 18 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: 12 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	11-19	9
α-helix	23-26	4
β-strand	35-36	2	1
α-helix	37-39	3
α-helix	43-46	4
β-strand	72-76	5	2
α-helix	79-81	3
β-strand	82-83	2	1
β-strand	86-91	6	2
α-helix	100-109	10
α-helix	111-117	7
β-strand	125	1	2
β-strand	128-132	5	2
β-strand	140-145	6	2
α-helix	146-148	3
α-helix	157-174	18
β-strand	179-182	4	2
α-helix	194-212	19
α-helix	213-215	3
β-strand	218-223	6	2
α-helix	226-240	15

Chain B: 13 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	11-19	9
α-helix	23-27	5
β-strand	35-36	2	3
α-helix	37-39	3
α-helix	41-42	2
α-helix	43-46	4
β-strand	72-76	5	4
α-helix	79-81	3
β-strand	82-83	2	3
β-strand	86-91	6	4
α-helix	100-109	10
α-helix	111-118	8
β-strand	125	1	4
β-strand	128-132	5	4
β-strand	140-145	6	4
α-helix	146-148	3
α-helix	155-174	20
β-strand	179-182	4	4
α-helix	194-212	19
α-helix	213-215	3
β-strand	218-223	6	4
α-helix	226-240	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
O-acetyl-ADP-ribose deacetylase MACROD2	A, B	protein	240	Homo sapiens	A1Z1Q3 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4IQY_1 O-acetyl-ADP-ribose deacetylase MACROD2 (chains A, B)
GHMKKKVWREEKERLLKMTLEERRKEYLRDYIPLNSILSWKEEMKGKGQNDEENTQETSQ
VKKSLTEKVSLYRGDITLLEVDAIVNAANASLLGGGGVDGCIHRAAGPCLLAECRNLNGC
DTGHAKITCGYDLPAKYVIHTVGPIARGHINGSHKEDLANCYKSSLKLVKENNIRSVAFP
CISTGIYGFPNEPAAVIALNTIKEWLAKNHHEVDRIIFCVFLEVDFKIYKKKMNEFFSVD

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
AR6	[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl[hydroxy-[…	C15 H23 N5 O14 P2	2

Primary citation

A family of macrodomain proteins reverses cellular mono-ADP-ribosylation. Jankevicius, G., Hassler, M., Golia, B. et al. Nat Struct Mol Biol (2013) 20:508-514. DOI 10.1038/nsmb.2523 · PubMed

Other PDB entries of the same protein (UniProt A1Z1Q3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6Y73 1.7 Å, The crystal structure of human MACROD2 in space group P43
6Y4Y 1.75 Å, The crystal structure of human MACROD2 in space group P41212
6Y4Z 1.9 Å, The crystal structure of human MACROD2 in space group P43212

Browse structure collections

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