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Crystal structure of uncharacterized protein from deinococcus radiodurans. northeast structural genomics consortium target DRR162B.

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

PDB: 3GW4
Type: protein
Length: 389 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q9RRX4
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	192	82% helix, 0% strand	Q9RRX4
B	Uncharacterized protein	protein	197	80% helix, 0% strand	Q9RRX4

Pockets

5 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	945	0.74	0.77	89	empty
2	78	0.46	0.81	16	empty
3	100	0.45	0.79	16	empty
4	64	0.44	0.82	14	empty
5	56	0.30	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 1693 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3GW4 · Crystal structure of uncharacterized protein from Deinococcus radiodurans. Northeast… · 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 Q9RRX4
Elsewhere: RCSB PDB 3GW4 · PDBe 3GW4 · UniProt Q9RRX4

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