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Yhea from bacillus subtilis

Analyse Yhea from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OEE
Type: protein
Length: 185 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: UPF0342 protein yhea
UniProt: O07542
Ligands: CA
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 88% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	UPF0342 protein yhea	protein	92	87% helix, 0% strand	O07542
B	UPF0342 protein yhea	protein	93	89% helix, 0% strand	O07542

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	551	0.67	0.77	50	empty
2	76	0.34	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 501 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

2OEE · yheA from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
O07542 · AlphaFold monomer V2.0 prediction for UPF0342 protein yhea (O07542) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 O07542
Elsewhere: RCSB PDB 2OEE · PDBe 2OEE · UniProt O07542

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