6ASR: REV1 UBM2 domain complex with ubiquitin

REV1 UBM2 domain complex with ubiquitin. Determined by X-ray diffraction at 2.36 Å resolution. Released 20 Jun 2018.

Method: X-ray diffraction
Resolution: 2.36 Å
Organism: Homo sapiens
Chains: 3
Atoms: 1,553
Mol. weight: 22.81 kDa
Ligands: NI
Released: 20 Jun 2018

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

Secondary structure: helices and β-sheets

6ASR contains 13 α-helices and 14 β-strands across 3 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: 5 helices, 7 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	72-73	2

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	1004-1009	6
α-helix	1013-1015	3
α-helix	1018-1022	5
α-helix	1026-1037	12

Chain C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	3
β-strand	12-16	5	3
β-strand	22	1	4
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	3
β-strand	48-49	2	3
α-helix	50-51	2
β-strand	55	1	4
α-helix	57-59	3
β-strand	66-71	6	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin	A, C	protein	76	Homo sapiens	P0CG47 (AlphaFold model)
DNA repair protein REV1	B	protein	51	Homo sapiens	Q9UBZ9 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6ASR_1 Ubiquitin (chains A, C)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Sequence of entity 2 (B), FASTA

>6ASR_2 DNA repair protein REV1 (chains B)
GSIKSSGLESNSDAGINLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ

Ligands and cofactors

ID	Name	Formula	Copies
NI	Nickel (II) ion	Ni	4

Primary citation

Structures of REV1 UBM2 Domain Complex with Ubiquitin and with a Small-Molecule that Inhibits the REV1 UBM2-Ubiquitin Interaction. Vanarotti, M., Grace, C.R., Miller, D.J. et al. J Mol Biol (2018) 430:2857-2872. DOI 10.1016/j.jmb.2018.05.042 · PubMed

Other PDB entries of the same protein (UniProt P0CG47 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NVG 1.07 Å, Thr12 Phosphorylated Ubiquitin
5TOG 1.08 Å, Room temperature structure of ubiquitin variant u7ub25.2540
5TOF 1.12 Å, Room temperature structure of ubiquitin variant u7ub25
4XOF 1.15 Å, Observing the overall rocking motion of a protein in a crystal - Orthorhombic Ubiquitin…
5GOD 1.15 Å, Lys27-linked di-ubiquitin
5GOB 1.15 Å, Lys6-linked di-ubiquitin
5W46 1.18 Å, Structure of S65D Phosphomimetic Ubiquitin Refined at 1.2 Angstroms Resolution
7S6O 1.25 Å, The crystal structure of Lys48-linked di-ubiquitin
8IC9 1.25 Å, Lys48-linked K48C-diubiquitin
5DK8 1.32 Å, Human ubiquitin in the P1 space group
7CAP 1.33 Å, Cyclic Lys48-linked triubiquitin
5V1Y 1.42 Å, Crystal structure of the ternary RPN13 PRU-RPN2 (940-953)-ubiquitin complex

Browse structure collections

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