Research workbench

MoxR AAA-ATPase RavA, spiral open ring conformation

Analyse MoxR AAA-ATPase RavA, spiral open ring conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SZB
Type: protein
Length: 2,886 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 7.0
Source: Escherichia coli K-12
Molecule: RavA + Mg-ADP
UniProt: P31473
Ligands: ADP
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · resolution 7.0 · 1 distinct chain · 41% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D, C, B, A, F, E	RavA + Mg-ADP	protein	481	41% helix, 14% strand	P31473

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains D, E, C, B, A, F

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	968	0.82	0.83	93	ADP
2	966	0.81	0.83	94	ADP
3	809	0.80	0.84	78	ADP
4	791	0.80	0.84	73	ADP
5	814	0.80	0.83	76	ADP

Interfaces

6 interfaces between chains.

B–A · 1602 Å² buried · 16 hydrogen bonds · protein-protein
C–B · 1588 Å² buried · 15 hydrogen bonds · protein-protein
D–E · 1577 Å² buried · 17 hydrogen bonds · protein-protein
F–E · 1565 Å² buried · 16 hydrogen bonds · protein-protein
D–C · 1560 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6SZB · Moxr aaa-ATPase rava, spiral open ring conformation · the same entry in another collection · chain C against C, TM-score 1.00
P31473 · AlphaFold monomer V2.0 prediction for ATPase rava (P31473) · a predicted model of the same protein · chain D against A, TM-score 0.82

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 P31473
Elsewhere: RCSB PDB 6SZB · PDBe 6SZB · UniProt P31473

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