2GBM: 35-36 8 Glycine Insertion Mutant of Ubiquitin

Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin. Determined by X-ray diffraction at 1.55 Å resolution. Released 16 May 2006.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,815
Mol. weight: 36.36 kDa
Ligands: ARS
Released: 16 May 2006

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

Secondary structure: helices and β-sheets

2GBM contains 16 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: 3 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	23-33	11
α-helix	46-48	3
β-strand	49-53	5	1
β-strand	56-57	2	1
β-strand	63	1	2
α-helix	65-67	3
β-strand	74-79	6	1

Chain B: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	3
β-strand	12-16	5	3
β-strand	22	1	4
α-helix	23-31	9
α-helix	32-36	5
α-helix	46-48	3
β-strand	49-53	5	3
β-strand	56-57	2	3
α-helix	58-59	2
β-strand	63	1	4
α-helix	65-67	3
β-strand	74-79	6	3

Chain C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	5
β-strand	12-16	5	5
β-strand	22	1	6
α-helix	23-33	11
α-helix	46-48	3
β-strand	49-53	5	5
β-strand	56-57	2	5
α-helix	58-59	2
β-strand	63	1	6
α-helix	65-67	3
β-strand	74-79	6	5

Chain D: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	7
β-strand	12-16	5	7
β-strand	22	1	8
α-helix	23-35	13
α-helix	46-48	3
β-strand	49-53	5	7
β-strand	56-57	2	7
α-helix	58-59	2
β-strand	63	1	8
α-helix	65-67	3
β-strand	74-79	6	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin	A, B, C, D	protein	84	Homo sapiens	P0CG48 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2GBM_1 Ubiquitin (chains A, B, C, D)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGGGGGGGGGIPPDQQRLIFAGKQLED
GRTLSDYNIQKESTLHLVLRLRGG

Ligands and cofactors

ID	Name	Formula	Copies
ARS	Arsenic	As	3

Primary citation

Structures of Ubiquitin Insertion Mutants Support Site-specific Reflex Response to Insertions Hypothesis. Ferraro, D.M., Ferraro, D.J., Ramaswamy, S. et al. J Mol Biol (2006) 359:390-402. DOI 10.1016/j.jmb.2006.03.047 · 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

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