2GYT: SAM (sterile alpha motif) domain of DLC1

Solution structure of the SAM (sterile alpha motif) domain of DLC1 (deleted in liver cancer 1). Determined by solution NMR. Released 24 Apr 2007.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 625
Mol. weight: 8.97 kDa
Released: 24 Apr 2007

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

Secondary structure: helices and β-sheets

2GYT contains 4 α-helices and 0 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: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	8-26	19
α-helix	29-38	10
α-helix	44-50	7
α-helix	56-74	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Deleted in liver cancer 1 protein, isoform 2	A	protein	76	Homo sapiens	Q96QB1 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2GYT_1 Deleted in liver cancer 1 protein, isoform 2 (chains A)
MCRKKPDTMILTQIEAKEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIE
ALCRRLNTLNKCAVMK

Primary citation

The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell migration. Zhong, D., Zhang, J., Yang, S. et al. J Cell Sci (2009) 122:414-424. DOI 10.1242/jcs.027482 · PubMed

Other PDB entries of the same protein (UniProt Q96QB1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5FZT 2.1 Å, The crystal structure of R7R8 in complex with a DLC1 fragment.
3KUQ 2.3 Å, Crystal structure of the DLC1 RhoGAP domain
7TPB 3.2 Å, p120RasGAP SH3 domain in complex with DLC1 RhoGAP domain
2DKY Solution structure of the SAM-domain of Rho-GTPase-activating protein 7
2KAP Solution structure of DLC1-SAM
2LOZ The novel binding mode of DLC1 and Tensin2 PTB domain

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