2ZVO: NEMO CoZi domain

NEMO CoZi domain in complex with diubiquitin in C2 space group. Determined by X-ray diffraction at 2.9 Å resolution. Released 24 Mar 2009.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Homo sapiens, Mus musculus
Chains: 4
Atoms: 3,965
Mol. weight: 55.91 kDa
Released: 24 Mar 2009

Explore 2ZVO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ZVO contains 20 α-helices and 28 β-strands across 4 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: 9 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	1
β-strand	12-16	5	1
β-strand	22	1	2
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	1
β-strand	48-49	2	1
α-helix	50-51	2
β-strand	55	1	2
α-helix	57-59	3
β-strand	66-71	6	1
α-helix	72	1
β-strand	77-83	7	3
β-strand	88-93	6	3
β-strand	98	1	4
α-helix	100-110	11
α-helix	114-116	3
β-strand	117-121	5	3
β-strand	124-125	2	3
α-helix	126	1
β-strand	131	1	4
α-helix	133-135	3
β-strand	142-147	6	3

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	254-288	35
α-helix	291-336	46

Chain D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	252-288	37
α-helix	290-324	35
α-helix	327-335	9

Chain G: 6 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	5
β-strand	12-16	5	5
β-strand	22	1	6
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	5
β-strand	48-49	2	5
β-strand	55	1	6
α-helix	65	1
β-strand	66-71	6	5
β-strand	77-82	6	7
β-strand	88-93	6	7
β-strand	98	1	8
α-helix	99-110	12
α-helix	114-116	3
β-strand	119-120	2	7
β-strand	125	1	7
β-strand	131	1	8
α-helix	137-138	2
β-strand	142-145	4	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
UBC protein	A, G	protein	154	Homo sapiens	P0CG48 (AlphaFold model)
NF-kappa-B essential modulator	B, D	protein	92	Mus musculus	O88522 (AlphaFold model)

Sequence of entity 1 (A, G), FASTA

>2ZVO_1 UBC protein (chains A, G)
GSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSD
YNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQR
LIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG

Sequence of entity 2 (B, D), FASTA

>2ZVO_2 NF-kappa-B essential modulator (chains B, D)
GSGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAAQHAIVMETVPVLKAQADIYKADFQA
ERHAREKLVEKKEYLQEQLEQLQREFNKLKVG

Primary citation

Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation. Rahighi, S., Ikeda, F., Kawasaki, M. et al. Cell (2009) 136:1098-1109. DOI 10.1016/j.cell.2009.03.007 · PubMed

Other PDB entries of the same protein (UniProt P0CG48 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6Q00 0.85 Å, TDP2 UBA Domain Bound to Ubiquitin at 0.85 Angstroms Resolution, Crystal Form 1
1OGW 1.32 Å, Synthetic Ubiquitin with fluoro-Leu at 50 and 67
5NL4 1.32 Å, Crystal structure of Zn1.3-E16V human ubiquitin (hUb) mutant adduct, from a solution 35…
2GBJ 1.35 Å, Crystal Structure of the 9-10 8 Glycine Insertion Mutant of Ubiquitin.
4HK2 1.4 Å, U7Ub25.2540
9FJ3 1.4 Å, Structure of ubiquitin bound of coiled-coil UIM form 2
1XD3 1.45 Å, Crystal structure of UCHL3-UbVME complex
4IUM 1.45 Å, Equine arteritis virus papain-like protease 2 (PLP2) covalently bound to ubiquitin
7UV5 1.45 Å, The crystal structure of Papain-Like Protease of SARS CoV-2, C111S/D286N mutant, in…
5NLF 1.5 Å, Crystal structure of Zn2.7-E16V human ubiquitin (hUb) mutant adduct, from a solution 100…
9F6G 1.5 Å, Human USP30 chimera bound to Ubiquitin-PA
9OVX 1.5 Å, Crystal structure of ubiquitin K27M mutant

Browse structure collections

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