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Solution structure of the arfgap domain of ADP-ribosylation factor gtpaseactivating protein 3 (arfgap 3)

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

PDB: 2CRW
Type: protein
Length: 149 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosylation factor GTPase-activating protein 3
UniProt: Q9NP61
Ligands: ZN
Pockets: 2 · best druggability 0.29

Structure

solution nmr · 1 distinct chain · 44% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADP-ribosylation factor GTPase-activating protein 3	protein	149	44% helix, 5% strand	Q9NP61

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.29	0.74	14	empty
2	50	0.28	0.75	16	empty

Compared structures

2CRW · Solution structure of the ArfGap domain of ADP-ribosylation factor GTPaseactivating… · the same entry in another collection · chain A against A, TM-score 1.00
Q9NP61 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor GTPase- activating protein… · a predicted model of the same protein · chain A against A, TM-score 0.86

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 Q9NP61
Elsewhere: RCSB PDB 2CRW · PDBe 2CRW · UniProt Q9NP61

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