6WO0: Protein artemis

human Artemis/SNM1C catalytic domain, crystal form 1. Determined by X-ray diffraction at 1.97 Å resolution. Released 1 Jul 2020.

Method: X-ray diffraction
Resolution: 1.97 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,040
Mol. weight: 43.61 kDa
Ligands: ZN
Released: 1 Jul 2020

Explore 6WO0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6WO0 contains 18 α-helices and 23 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: 18 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	14-16	3	1
α-helix	21-25	5
β-strand	28-30	3	1
α-helix	36-38	3
α-helix	45-53	9
β-strand	59-61	3	1
α-helix	63-69	7
α-helix	73-78	6
β-strand	82-84	3	1
β-strand	91-96	6	2
β-strand	103-112	10	2
β-strand	120-126	7	2
β-strand	129-133	5	2
α-helix	144-146	3
α-helix	148-150	3
β-strand	151-152	2	3
β-strand	155-156	2	3
β-strand	161-164	4	2
α-helix	171-173	3
β-strand	175	1	4
α-helix	179-194	16
β-strand	200-204	5	5
α-helix	213-223	11
α-helix	226	1
β-strand	227-228	2	5
α-helix	233-235	3
α-helix	239-242	4
β-strand	245-246	2	5
β-strand	253-254	2	5
α-helix	261-266	6
β-strand	276-277	2	6
β-strand	280-281	2	6
α-helix	282	1
β-strand	283-290	8	5
β-strand	294	1	4
β-strand	304-308	5	5
β-strand	311-315	5	5
α-helix	322-332	11
β-strand	336-339	4	2
α-helix	348-355	8
α-helix	356-358	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein artemis	A	protein	375	Homo sapiens	Q96SD1 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6WO0_1 Protein artemis (chains A)
SSFEGQMAEYPTISIDRFDRENLRARAYFLSHCHKDHMKGLRAPTLKRRLECSLKVYLYC
SPVTKELLLTSPKYRFWKKRIISIEIETPTQISLVDEASGEKEEIVVTLLPAGHCPGSVM
FLFQGNNGTVLYTGDFRLAQGEAARMELLHSGGRVKDIQSVYLDTTFCDPRFYQIPSREE
CLSGVLELVRSWITRSPYHVVWLNCKAAYGYEYLFTNLSEELGVQVHVNKLDMFRNMPEI
LHHLTTDRNTQIHACRHPKAEEYFQWSKLPCGITSRNRIPLHIISIKPSTMWFGERSRKT
NVIVRTGESSYRACFSFHSSYSEIKDFLSYLCPVNAYPNVIPVGTTMDKVVEILKPLCRS
SQSTEPKKGENLYFQ

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

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

Primary citation

Structural analysis of the catalytic domain of Artemis endonuclease/SNM1C reveals distinct structural features. Karim, M.F., Liu, S., Laciak, A.R. et al. J Biol Chem (2020) 295:12368-12377. DOI 10.1074/jbc.RA120.014136 · PubMed

Other PDB entries of the same protein (UniProt Q96SD1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6TT5 1.5 Å, Crystal structure of DCLRE1C/Artemis
7AFU 1.56 Å, The structure of Artemis variant H33A
7AF1 1.7 Å, The structure of Artemis/SNM1C/DCLRE1C with 2 Zinc ions
7AFS 1.7 Å, The structure of Artemis variant D37A
7AGI 1.7 Å, The structure of Artemis variant H35D
7APV 1.95 Å, Structure of Artemis/DCLRE1C/SNM1C in complex with Ceftriaxone
7ABS 1.97 Å, Structure of human DCLRE1C/Artemis in complex with DNA - re-evaluation of 6WO0
4HTP 2.25 Å, Crystal structure of the DBD domain of human DNA ligase IV bound to Artemis peptide
6WNL 2.37 Å, human Artemis/SNM1C catalytic domain, crystal form 2
3W1B 2.4 Å, Crystal Structure of Human DNA ligase IV-Artemis Complex (Mercury Derivative)
3W1G 2.55 Å, Crystal Structure of Human DNA ligase IV-Artemis Complex (Native)
7SGL 3.0 Å, DNA-PK complex of DNA end processing

Browse structure collections

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