1LB1: Dbl and Pleckstrin homology domains of Dbs

Crystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA. Determined by X-ray diffraction at 2.81 Å resolution. Released 29 May 2002.

Method: X-ray diffraction
Resolution: 2.81 Å
Organisms: Mus musculus, Homo sapiens
Chains: 8
Atoms: 16,236
Mol. weight: 251.35 kDa
Released: 29 May 2002

Explore 1LB1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LB1 contains 126 α-helices and 72 β-strands across 8 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.

Chains A and G: 22 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	625-654	30
α-helix	655-659	5
α-helix	660-663	4
α-helix	665-670	6
α-helix	673-677	5
α-helix	679-683	5
α-helix	686-691	6
α-helix	692-697	6
α-helix	698-702	5
α-helix	708-711	4
α-helix	712-716	5
α-helix	721-723	3
α-helix	724-742	19
α-helix	746-755	10
α-helix	761-765	5
α-helix	767-772	6
α-helix	775-784	10
α-helix	792-815	24
β-strand	818-819	2	1
α-helix	826-828	3
β-strand	831-841	11	1
β-strand	859-866	8	1
β-strand	869-876	8	1
α-helix	883-885	3
β-strand	888-896	9	1
α-helix	897-899	3
β-strand	900-903	4	1
β-strand	906	1	2
β-strand	909	1	2
β-strand	912-917	6	1
β-strand	922-927	6	1
α-helix	931-951	21

Chains B, D, F and H: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	3
α-helix	18-27	10
β-strand	42-48	7	3
β-strand	51-58	8	3
α-helix	70-73	4
β-strand	79-82	4	3
β-strand	83-85	3	4
α-helix	89-94	6
α-helix	95-99	5
α-helix	100-106	7
β-strand	112	1	3
β-strand	113-117	5	4
α-helix	119-121	3
α-helix	125-133	9
α-helix	141-151	11
β-strand	155-158	4	4
α-helix	167-179	13

Chain C: 23 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	625-654	30
α-helix	655-659	5
α-helix	660-663	4
α-helix	665-670	6
α-helix	673-677	5
α-helix	679-683	5
α-helix	686-691	6
α-helix	692-697	6
α-helix	698-702	5
α-helix	708-710	3
α-helix	711-716	6
α-helix	721-723	3
α-helix	724-742	19
α-helix	746-755	10
α-helix	761-765	5
α-helix	767-772	6
α-helix	775-784	10
α-helix	792-815	24
β-strand	818-819	2	5
α-helix	826-828	3
β-strand	831-841	11	5
β-strand	859-866	8	5
β-strand	869-876	8	5
α-helix	883-885	3
β-strand	888-896	9	5
α-helix	897-899	3
β-strand	900-903	4	5
β-strand	906	1	6
β-strand	909	1	6
β-strand	912-917	6	5
α-helix	918-920	3
β-strand	922-927	6	5
α-helix	931-951	21

Chain E: 23 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	625-654	30
α-helix	655-659	5
α-helix	660-663	4
α-helix	665-670	6
α-helix	673-677	5
α-helix	679-683	5
α-helix	686-691	6
α-helix	692-697	6
α-helix	698-702	5
α-helix	708-711	4
α-helix	712-716	5
α-helix	721-723	3
α-helix	724-742	19
α-helix	746-755	10
α-helix	761-765	5
α-helix	767-772	6
α-helix	775-784	10
α-helix	792-815	24
β-strand	818-819	2	9
α-helix	826-828	3
β-strand	831-841	11	9
β-strand	859-866	8	9
β-strand	869-876	8	9
α-helix	883-885	3
β-strand	888-896	9	9
α-helix	897-899	3
β-strand	900-903	4	9
β-strand	906	1	10
β-strand	909	1	10
β-strand	912-917	6	9
α-helix	918-920	3
β-strand	922-927	6	9
α-helix	931-951	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide exchange factor DBS	A, C, E, G	protein	353	Mus musculus	Q64096 (AlphaFold model)
Transforming protein RhoA	B, D, F, H	protein	192	Homo sapiens	P61586 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>1LB1_1 Guanine nucleotide exchange factor DBS (chains A, C, E, G)
MGEEEESLAILRRHVMNELLDTERAYVEELLCVLEGYAAEMDNPLMAHLISTGLQNKKNI
LFGNMEEIYHFHNRIFLRELESCIDCPELVGRCFLERMEEFQIYEKYCQNKPRSESLWRQ
CSDCPFFQECQKKLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSKHCEGAEDLQEALSS
ILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWTDHKKGHTKVKELARFKPMQR
HLFLHEKAVLFCKKREENGEGYEKAPSYSYKQSLNMTAVGITENVKGDTKKFEIWYNARE
EVYIIQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRALEQSHSLEHHHHHH

Sequence of entity 2 (B, D, F, H), FASTA

>1LB1_2 Transforming protein RhoA (chains B, D, F, H)
GAMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALW
DTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNK
KDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAA
LQARRGKKKSGS

Primary citation

Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Snyder, J.T., Worthylake, D.K., Rossman, K.L. et al. Nat Struct Biol (2002) 9:468-475. DOI 10.1038/nsb796 · PubMed

Other PDB entries of the same protein (UniProt Q64096 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1KZ7 2.4 Å, Crystal Structure of the DH/PH Fragment of Murine Dbs in Complex with the Placental…
1KZG 2.6 Å, DbsCdc42(Y889F)
1RJ2 3.0 Å, Crystal structure of the DH/PH fragment of Dbs without bound GTPase

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