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Structure of human ADP-ribosylation factor 4

Analyse Structure of human ADP-ribosylation factor 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Z6X
Type: protein
Length: 350 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosylation factor 4
UniProt: P18085
Ligands: GDP, MG
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ADP-ribosylation factor 4	protein	175	35% helix, 29% strand	P18085

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 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	661	0.67	0.76	69	MG, GDP
2	50	0.32	0.77	12	empty

Interfaces

1 interface between chains.

A–B · 603 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1Z6X · Structure Of Human ADP-Ribosylation Factor 4 · the same entry in another collection · chain A against A, TM-score 1.00
P18085 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor 4 (P18085) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 P18085
Elsewhere: RCSB PDB 1Z6X · PDBe 1Z6X · UniProt P18085

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