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Ohr from xylella fastidiosa in oxidized state

Analyse Ohr from xylella fastidiosa in oxidized state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XX2
Type: protein
Length: 423 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Organic hydroperoxide resistance protein
EC: 1.-.-.-
UniProt: Q9PCF4
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Organic hydroperoxide resistance protein (EC 1.-.-.-)	protein	141	33% helix, 28% strand	Q9PCF4

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	245	0.68	0.84	32	empty
2	220	0.66	0.84	32	empty
3	376	0.62	0.78	44	empty

Interfaces

3 interfaces between chains.

B–C · 3281 Å² buried · 52 hydrogen bonds · protein-protein
A–B · 277 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 67 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

4XX2 · Ohr from Xylella fastidiosa in oxidized state · 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 Q9PCF4
Elsewhere: RCSB PDB 4XX2 · PDBe 4XX2 · UniProt Q9PCF4

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