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Crystal structure of the CRARL6DN in the GDP bound form

Analyse Crystal structure of the CRARL6DN in the GDP bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4V0K
Type: protein
Length: 315 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arf-like small GTPase
UniProt: A8JF99
Ligands: GDP, CD
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arf-like small GTPase	protein	151	36% helix, 25% strand	A8JF99
B	Arf-like small GTPase	protein	164	33% helix, 21% strand	A8JF99

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
CD · Cadmium ion · metal · 10 copies · chains A, B

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

Pockets

2 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	212	0.63	0.83	33	empty
2	50	0.24	0.73	14	CD

Interfaces

1 interface between chains.

A–B · 380 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4V0K · Crystal structure of the CrARL6DN in the GDP bound form · the same entry in another collection · chain A against A, TM-score 1.00

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 A8JF99
Elsewhere: RCSB PDB 4V0K · PDBe 4V0K · UniProt A8JF99

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