6TT5: DCLRE1C/Artemis

Crystal structure of DCLRE1C/Artemis. Determined by X-ray diffraction at 1.5 Å resolution. Released 12 Feb 2020.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,178
Mol. weight: 42.33 kDa
Ligands: NI, ZN
Released: 12 Feb 2020

Explore 6TT5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TT5 contains 17 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 AAA: 17 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	63-70	8
α-helix	73-81	9
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
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	AAA	protein	362	Homo sapiens	Q96SD1 (AlphaFold model)

Sequence of entity 1 (AAA), FASTA

>6TT5_1 Protein artemis (chains AAA)
SMSSFEGQMAEYPTISIDRFDRENLRARAYFLSHCHKDHMKGLRAPTLKRRLECSLKVYL
YCSPVTKELLLTSPKYRFWKKRIISIEIETPTQISLVDEASGEKEEIVVTLLPAGHCPGS
VMFLFQGNNGTVLYTGDFRLAQGEAARMELLHSGGRVKDIQSVYLDTTFCDPRFYQIPSR
EECLSGVLELVRSWITRSPYHVVWLNCKAAYGYEYLFTNLSEELGVQVHVNKLDMFRNMP
EILHHLTTDRNTQIHACRHPKAEEYFQWSKLPCGITSRNRIPLHIISIKPSTMWFGERSR
KTNVIVRTGESSYRACFSFHSSYSEIKDFLSYLCPVNAYPNVIPVGTTMDKVVEILKPLC
RS

Ligands and cofactors

ID	Name	Formula	Copies
NI	Nickel (II) ion	Ni	1
ZN	Zinc ion	Zn	2

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

Primary citation

Structural and mechanistic insights into the Artemis endonuclease and strategies for its inhibition. Yosaatmadja, Y., Baddock, H.T., Newman, J.A. et al. Nucleic Acids Res (2021) 49:9310-9326. DOI 10.1093/nar/gkab693 · PubMed

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

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
6WO0 1.97 Å, human Artemis/SNM1C catalytic domain, crystal form 1
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

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