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Crystal structure of the catalytic and ATP-binding domain from vras in complex with ADP

Analyse Crystal structure of the catalytic and ATP-binding domain from vras in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GT8
Type: protein
Length: 133 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sensor protein vras
EC: 2.7.13.3
UniProt: Q7A2Q0
Ligands: ADP, MG
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sensor protein vras (EC 2.7.13.3)	protein	133	41% helix, 29% strand	Q7A2Q0

Ligands and binding sites

ADP · Adenosine-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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.50	0.82	23	ADP, MG

Compared structures

4GT8 · Crystal Structure of the Catalytic and ATP-binding Domain from VraS in Complex with ADP · the same entry in another collection · chain A against A, TM-score 1.00
Q7A2Q0 · AlphaFold monomer V2.0 prediction for sensor protein vras (Q7A2Q0) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q7A2Q0
Elsewhere: RCSB PDB 4GT8 · PDBe 4GT8 · UniProt Q7A2Q0

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