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Structure of the heme binding protein chux

Analyse Structure of the heme binding protein chux in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OVI
Type: protein
Length: 628 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein chux
UniProt: Q8X5N5
Pockets: 9 · best druggability 0.61

Structure

x-ray diffraction · 3 distinct chains · 29% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein chux	protein	158	29% helix, 37% strand	Q8X5N5
C	Hypothetical protein chux	protein	156	28% helix, 38% strand	Q8X5N5
D	Hypothetical protein chux	protein	156	30% helix, 36% strand	Q8X5N5

Pockets

9 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	305	0.61	0.78	37	empty
2	280	0.59	0.78	31	empty
3	302	0.53	0.75	35	empty
4	205	0.51	0.77	36	empty
5	161	0.50	0.78	32	empty

Interfaces

4 interfaces between chains.

A–D · 1032 Å² buried · 21 hydrogen bonds · protein-protein
B–C · 994 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 571 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 88 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2OVI · Structure of the Heme Binding Protein ChuX · 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 Q8X5N5
Elsewhere: RCSB PDB 2OVI · PDBe 2OVI · UniProt Q8X5N5

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