2OM2: Human G[alpha]i1

Crystal Structure Of Human G[alpha]i1 Bound To The Goloco Motif Of Rgs14. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Jul 2007.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
4
Atoms
6,039
Mol. weight
83.44 kDa
Ligands
GDP, MG
Released
10 Jul 2007

Explore 2OM2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OM2 contains 46 α-helices and 14 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: 20 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand33-4081
α-helix46-5712
α-helix63-675
α-helix70-9021
α-helix100-11314
α-helix1151
α-helix121-13212
α-helix134-1407
α-helix143-1453
α-helix152-1576
α-helix159-1635
α-helix171-1766
β-strand185-19061
β-strand195-20061
α-helix208-2158
β-strand220-22671
α-helix227-2315
α-helix232-2354
α-helix242-25514
α-helix257-2593
β-strand263-26971
α-helix271-2777
α-helix283-2853
α-helix296-30813
β-strand319-32351
α-helix329-34618
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix498-50811
α-helix525-5273
α-helix528-5303
Chain C: 19 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand1033-103972
α-helix1048-105710
α-helix1063-10686
α-helix1070-109021
α-helix1100-111314
β-strand111513
β-strand111813
α-helix1121-113212
α-helix1134-11407
α-helix1143-11453
α-helix1152-11565
α-helix1159-11624
α-helix1171-11755
β-strand1185-119172
β-strand1194-120072
α-helix1208-12158
β-strand1220-122562
α-helix1228-12314
α-helix1232-12354
α-helix1242-125514
α-helix1257-12593
β-strand1263-126862
α-helix1271-12777
α-helix1283-12853
α-helix1296-130813
β-strand1319-132352
α-helix1329-134517
Chain D: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1497-150913
α-helix1521-15244
α-helix1525-15273
α-helix1528-15303

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Guanine nucleotide-binding protein G(i), alpha-1 subunitA, Cprotein325Homo sapiensP63096 (AlphaFold model)
Regulator of G-protein signalling 14 GoLoco motif peptideB, Dprotein36O43566 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>2OM2_1 Guanine nucleotide-binding protein G(i), alpha-1 subunit (chains A, C)
GAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMG
RLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLN
DSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERK
KWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLN
KKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDT
KNVQFVFDAVTDVIIKNNLKDCGLF
Sequence of entity 2 (B, D), FASTA
>2OM2_2 Regulator of G-protein signalling 14 GoLoco motif peptide (chains B, D)
DIEGLVELLNRVQSSGAHDQRGLLRKEDLVLPEFLQ

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22
MGMagnesium ionMg2

Primary citation

Structure-based Protocol for Identifying Mutations that Enhance Protein-Protein Binding Affinities. Sammond, D.W., Eletr, Z.M., Purbeck, C. et al. J Mol Biol (2007) 371:1392-1404. DOI 10.1016/j.jmb.2007.05.096 · PubMed

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

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