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Crystal structure of GGDEF domain of the E. coli DosC - form III

Analyse Crystal structure of GGDEF domain of the E. coli DosC - form III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZVG
Type: protein
Length: 329 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.2
Source: Escherichia coli K-12
Molecule: Diguanylate cyclase DosC
EC: 2.7.7.65
UniProt: P0AA89
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.2 · 2 distinct chains · 48% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diguanylate cyclase DosC (EC 2.7.7.65)	protein	165	48% helix, 21% strand	P0AA89
B	Diguanylate cyclase DosC (EC 2.7.7.65)	protein	164	48% helix, 21% strand	P0AA89

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	58	0.69	0.97	19	empty
2	68	0.29	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 726 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4ZVG · Crystal structure of ggdef domain of the E. COLI dosc - form III · the same entry in another collection · chain A against A, TM-score 1.00
P0AA89 · AlphaFold monomer V2.0 prediction for diguanylate cyclase dosc (P0AA89) · 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 P0AA89
Elsewhere: RCSB PDB 4ZVG · PDBe 4ZVG · UniProt P0AA89

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