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Crystal structure of ddro from deinococcus geothermalis

Analyse Crystal structure of ddro from deinococcus geothermalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JQ1
Type: protein
Length: 259 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional regulator, xre family
UniProt: Q1J1J5
Ligands: LI
Pockets: 4 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional regulator, xre family	protein	129	57% helix, 2% strand	Q1J1J5
B	Transcriptional regulator, xre family	protein	130	56% helix, 2% strand	Q1J1J5

Ligands and binding sites

LI · Lithium ion · metal · 5 copies · chains A, B

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

Pockets

4 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	65	0.34	0.77	16	empty
2	63	0.32	0.76	19	empty
3	61	0.30	0.75	13	LI
4	57	0.30	0.75	14	LI

Interfaces

1 interface between chains.

A–B · 1726 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6JQ1 · Crystal Structure of DdrO from Deinococcus geothermalis · the same entry in another collection · chain A against A, 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 Q1J1J5
Elsewhere: RCSB PDB 6JQ1 · PDBe 6JQ1 · UniProt Q1J1J5

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