1Z2C: MDIA1 GBD-FH3

Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP. Determined by X-ray diffraction at 3.0 Å resolution. Released 10 May 2005.

Method
X-ray diffraction
Resolution
3.0 Å
Organisms
Homo sapiens, Mus musculus
Chains
4
Atoms
8,399
Mol. weight
133.56 kDa
Ligands
MG, GNP
Released
10 May 2005

Explore 1Z2C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Z2C contains 62 α-helices and 16 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: 11 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand4-1291
α-helix18-269
β-strand39-48101
β-strand51-60101
α-helix64-663
α-helix70-723
β-strand79-8571
α-helix89-946
α-helix95-995
α-helix100-1067
β-strand112-11761
α-helix119-1213
α-helix125-1328
α-helix138-1403
α-helix141-15010
β-strand155-15841
α-helix167-17812
Chain B: 21 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix84-929
α-helix98-1058
α-helix109-12113
α-helix136-1427
α-helix149-16517
α-helix168-19023
α-helix202-21615
α-helix219-2268
α-helix231-2377
α-helix244-25815
α-helix266-28015
α-helix287-2937
α-helix299-31315
α-helix319-33113
α-helix334-3396
α-helix341-3433
α-helix347-37731
α-helix381-3877
α-helix388-3925
α-helix398-40811
α-helix418-43417
Chain C: 11 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand4-1292
α-helix18-258
β-strand3913
β-strand42-4872
β-strand51-5882
β-strand6013
α-helix64-663
α-helix70-734
β-strand79-8572
α-helix89-946
α-helix95-995
α-helix100-1067
β-strand112-11762
α-helix119-1224
α-helix125-1339
α-helix138-1403
α-helix141-15010
β-strand155-15842
α-helix167-17711
Chain D: 19 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix86-938
α-helix102-1054
α-helix109-12113
α-helix138-1436
α-helix149-16517
α-helix168-18922
α-helix203-21513
α-helix219-2279
α-helix231-2377
α-helix244-25815
α-helix266-28116
α-helix287-2937
β-strand29514
β-strand29714
α-helix299-31315
α-helix319-33113
α-helix334-3418
α-helix347-37731
α-helix381-39111
α-helix398-40811
α-helix418-43316

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rho-related GTP-binding protein RhoCA, Cprotein193Homo sapiensP08134 (AlphaFold model)
Diaphanous protein homolog 1B, Dprotein383Mus musculusO08808 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>1Z2C_1 Rho-related GTP-binding protein RhoC (chains A, C)
MAAIRKKLVIVGDGACGKTCLLIVNSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD
LRQDEHTRRELAKMKQEPVRSEEGRDMANRISAFGYLECSAKTKEGVREVFEMATRAGLQ
VRKNKRRRGCPIL
Sequence of entity 2 (B, D), FASTA
>1Z2C_2 Diaphanous protein homolog 1 (chains B, D)
DPTAQSLQDISDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMN
QKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKR
LHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMI
DAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQL
INALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLK
GRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEEC
VSQIVLHKNGTDPDFKCRHLQID

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg3
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P32

Primary citation

Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Rose, R., Weyand, M., Lammers, M. et al. Nature (2005) 435:513-518. DOI 10.1038/nature03604 · PubMed

Other PDB entries of the same protein (UniProt P08134 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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