3UMR: G202D mutant of human G-alpha-i1

Crystal structure of the G202D mutant of human G-alpha-i1. Determined by X-ray diffraction at 2.04 Å resolution. Released 24 Oct 2012.

Method
X-ray diffraction
Resolution
2.04 Å
Organism
Homo sapiens
Chains
1
Atoms
2,981
Mol. weight
41.13 kDa
Ligands
GDP
Released
24 Oct 2012

Explore 3UMR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3UMR contains 22 α-helices and 7 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: 22 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix9-168
α-helix20-234
α-helix27-293
α-helix30-312
β-strand32-4091
α-helix46-5712
α-helix63-675
α-helix70-9122
α-helix100-11314
α-helix121-13212
α-helix134-1407
α-helix143-1453
α-helix152-1576
α-helix159-1624
α-helix171-1755
β-strand184-19181
β-strand194-20181
β-strand220-22671
α-helix227-2293
α-helix242-25413
α-helix257-2593
β-strand263-26971
α-helix271-2777
α-helix283-2853
α-helix296-30914
β-strand319-32351
α-helix329-34618
α-helix348-3503
β-strand35311

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Guanine nucleotide-binding protein G(i) subunit alpha-1Aprotein354Homo sapiensP63096 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3UMR_1 Guanine nucleotide-binding protein G(i) subunit alpha-1 (chains A)
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAG
YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT
AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK
TTGIVETHFTFKDLHFKMFDVDGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM
NRMHESMKLFDSICNNKCFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAA
AYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21

Water and common crystallization additives (SO4, CL, GOL) are not listed.

Primary citation

Structural Determinants Underlying the Temperature-sensitive Nature of a G-alpha Mutant in Asymmetric Cell Division of Caenorhabditis elegans. Johnston, C.A., Afshar, K., Snyder, J.T. et al. To be published.

Other PDB entries of the same protein (UniProt P63096 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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