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Sulfur-sad at long wavelength: structure of BH3703 from bacillus halodurans

Analyse Sulfur-sad at long wavelength: structure of BH3703 from bacillus halodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3I0T
Type: protein
Length: 341 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BH3703 protein
UniProt: Q9K6M5
Ligands: SO4
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BH3703 protein	protein	170	48% helix, 21% strand	Q9K6M5
B	BH3703 protein	protein	171	47% helix, 20% strand	Q9K6M5

Ligands and binding sites

SO4 · Sulfate ion · ion · 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	234	0.57	0.79	27	empty
2	65	0.36	0.78	16	SO4

Interfaces

1 interface between chains.

A–B · 1207 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

3I0T · Sulfur-SAD at long wavelength: Structure of BH3703 from Bacillus halodurans · 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 Q9K6M5
Elsewhere: RCSB PDB 3I0T · PDBe 3I0T · UniProt Q9K6M5

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