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Delta-17 human ADP ribosylation factor 1 complexed with GDP

Analyse Delta-17 human ADP ribosylation factor 1 complexed with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1U81
Type: protein
Length: 164 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosylation factor 1
UniProt: P84077
Ligands: GDP, MG
Pockets: 3 · best druggability 0.66

Structure

solution nmr · 1 distinct chain · 24% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADP-ribosylation factor 1	protein	164	24% helix, 18% strand	P84077

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.66	0.94	20	empty
2	76	0.48	0.82	19	empty
3	63	0.39	0.79	13	empty

Compared structures

1U81 · Delta-17 Human ADP Ribosylation Factor 1 Complexed with GDP · the same entry in another collection · chain A against A, TM-score 1.00
P84077 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor 1 (P84077) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 P84077
Elsewhere: RCSB PDB 1U81 · PDBe 1U81 · UniProt P84077

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