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Crystal structure of the SEC7 domain from human CYTOHESIN1

Analyse Crystal structure of the SEC7 domain from human CYTOHESIN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4A4P
Type: protein
Length: 372 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CYTOHESIN1
UniProt: Q15438
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	CYTOHESIN1	protein	186	65% helix, 2% strand	Q15438

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	714	0.74	0.79	59	empty
2	159	0.46	0.76	19	empty
3	76	0.43	0.80	15	empty
4	57	0.34	0.77	12	empty

Interfaces

1 interface between chains.

A–B · 624 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4A4P · crystal structure of the Sec7 domain from human cytohesin1 · the same entry in another collection · chain A against A, TM-score 1.00
Q15438 · AlphaFold monomer V2.0 prediction for cytohesin-1 (Q15438) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q15438
Elsewhere: RCSB PDB 4A4P · PDBe 4A4P · UniProt Q15438

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