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Bldd ctd-C-di-gmp complex

Analyse Bldd ctd-C-di-gmp complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OAZ
Type: protein
Length: 147 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative DNA-binding protein
UniProt: Q7AKQ8
Ligands: C2E
Pockets: 1 · best druggability 0.26

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
R	Putative DNA-binding protein	protein	72	57% helix, 11% strand	Q7AKQ8
A	Putative DNA-binding protein	protein	75	56% helix, 9% strand	Q7AKQ8

Ligands and binding sites

C2E · 9,9'-[(2r,3r,3as,5s,7ar,9r,10r,10as,12s,14ar)-3,5,10, 12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3, 2-D:3',2'-J][1,3,7,9,2, 8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) · ligand · 4 copies · chains R, 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.26	0.72	11	C2E

Interfaces

1 interface between chains.

R–A · 71 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4OAZ · BldD CTD-c-di-GMP complex · the same entry in another collection · chain R against R, TM-score 1.00

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 Q7AKQ8
Elsewhere: RCSB PDB 4OAZ · PDBe 4OAZ · UniProt Q7AKQ8

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