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The 2.6 ångström crystal structure of chbp, the cif homologue from burkholderia pseudomallei

Analyse The 2.6 ångström crystal structure of chbp, the cif homologue from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EIT
Type: protein
Length: 488 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative ATP/GTP binding protein
UniProt: Q63KH5
Pockets: 4 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative ATP/GTP binding protein	protein	244	48% helix, 13% strand	Q63KH5
B	Putative ATP/GTP binding protein	protein	244	47% helix, 13% strand	Q63KH5

Pockets

4 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	1134	0.86	0.87	113	empty
2	52	0.36	0.80	13	empty
3	56	0.30	0.75	17	empty
4	55	0.29	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 1462 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered, oxidation).

Compared structures

3EIT · the 2.6 angstrom crystal structure of CHBP, the Cif Homologue from Burkholderia… · 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 Q63KH5
Elsewhere: RCSB PDB 3EIT · PDBe 3EIT · UniProt Q63KH5

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