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Crystal structure of hyopthetical protein (GK_1056) from geobacillus kaustophilus HTA426

Analyse Crystal structure of hyopthetical protein (GK_1056) from geobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PQ0
Type: protein
Length: 513 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical conserved protein GK1056
UniProt: Q5L139
Pockets: 5 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical conserved protein GK1056	protein	256	39% helix, 23% strand	Q5L139
B	Hypothetical conserved protein GK1056	protein	257	39% helix, 22% strand	Q5L139

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	434	0.65	0.78	35	empty
2	295	0.60	0.79	38	empty
3	310	0.60	0.78	55	empty
4	90	0.50	0.83	22	empty
5	142	0.44	0.76	20	empty

Interfaces

1 interface between chains.

A–B · 1189 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 17 modified (engineered).

Compared structures

2PQ0 · Crystal structure of Hyopthetical protein (gk_1056) from geobacillus Kaustophilus HTA426 · 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 Q5L139
Elsewhere: RCSB PDB 2PQ0 · PDBe 2PQ0 · UniProt Q5L139

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