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Gmp-pnp bound dynamin-1-like protein GTPase-ged fusion

Analyse Gmp-pnp bound dynamin-1-like protein GTPase-ged fusion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H1V
Type: protein
Length: 358 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dynamin-1-like protein
EC: 3.6.5.5
UniProt: O00429
Ligands: GNP
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dynamin-1-like protein (EC 3.6.5.5)	protein	358	42% helix, 15% strand	O00429

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	383	0.64	0.78	52	GNP
2	103	0.62	0.88	21	empty
3	93	0.53	0.84	23	empty

Compared structures

4H1V · GMP-PNP bound dynamin-1-like protein GTPase-GED fusion · the same entry in another collection · chain A against A, TM-score 1.00
O00429 · AlphaFold monomer V2.0 prediction for dynamin-1-like protein (O00429) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 O00429
Elsewhere: RCSB PDB 4H1V · PDBe 4H1V · UniProt O00429

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