3EG5: MDIA1-TSH GBD-FH3

Crystal structure of MDIA1-TSH GBD-FH3 in complex with CDC42-GMPPNP. Determined by X-ray diffraction at 2.7 Å resolution. Released 14 Oct 2008.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Mus musculus
Chains: 4
Atoms: 8,341
Mol. weight: 129.1 kDa
Ligands: GNP, MG
Released: 14 Oct 2008

Explore 3EG5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EG5 contains 60 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

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	16-25	10
β-strand	37-46	10	1
β-strand	49-58	10	1
α-helix	62-64	3
α-helix	68-71	4
β-strand	77-83	7	1
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	1
α-helix	117-119	3
α-helix	123-131	9
α-helix	136-138	3
α-helix	139-148	10
β-strand	154-156	3	1
α-helix	165-177	13

Chains B and D: 19 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	85-93	9
α-helix	98-105	8
α-helix	109-122	14
α-helix	136-143	8
α-helix	149-165	17
α-helix	168-190	23
α-helix	202-215	14
α-helix	219-226	8
α-helix	231-237	7
α-helix	244-258	15
α-helix	266-281	16
α-helix	287-291	5
β-strand	295	1	2
β-strand	297	1	2
α-helix	299-313	15
α-helix	319-331	13
α-helix	334-341	8
α-helix	347-377	31
α-helix	381-391	11
α-helix	398-407	10
α-helix	418-433	16

Chain C: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	3
α-helix	16-25	10
β-strand	37-46	10	3
β-strand	49-58	10	3
α-helix	62-64	3
α-helix	68-71	4
β-strand	77-83	7	3
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	3
α-helix	117-121	5
α-helix	123-131	9
α-helix	136-138	3
α-helix	139-148	10
β-strand	154-156	3	3
α-helix	165-177	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division control protein 42 homolog	A, C	protein	178	Mus musculus	P60766 (AlphaFold model)
Protein diaphanous homolog 1	B, D	protein	383	Mus musculus	O08808 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>3EG5_1 Cell division control protein 42 homolog (chains A, C)
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAALE

Sequence of entity 2 (B, D), FASTA

>3EG5_2 Protein diaphanous homolog 1 (chains B, D)
DPTAQSLQDISDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMN
QKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLTSHPVSWVQTFGAEGLASLLDILKR
LHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMI
DAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQL
INALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLK
GRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEEC
VSQIVLHKNGTDPDFKCRHLQID

Ligands and cofactors

ID	Name	Formula	Copies
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	2
MG	Magnesium ion	Mg	2

Primary citation

Specificity of Interactions between mDia Isoforms and Rho Proteins. Lammers, M., Meyer, S., Kuhlmann, D. et al. J Biol Chem (2008) 283:35236-35246. DOI 10.1074/jbc.M805634200 · PubMed

Other PDB entries of the same protein (UniProt P60766 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5C2J 2.5 Å, Complex structure of the GAP domain of MgcRacGAP and Cdc42

Browse structure collections

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