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Crystal structure of protein BF1032 from bacteroides fragilis, northeast structural genomics consortium target BFR309

Analyse Crystal structure of protein BF1032 from bacteroides fragilis, northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NRH
Type: protein
Length: 310 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein BF1032
UniProt: Q64XJ4
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein BF1032	protein	158	74% helix, 4% strand	Q64XJ4
B	Uncharacterized protein BF1032	protein	152	75% helix, 3% strand	Q64XJ4

Pockets

4 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	257	0.76	0.89	32	empty
2	53	0.71	0.98	18	empty
3	246	0.58	0.79	22	empty
4	71	0.30	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 955 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3NRH · Crystal Structure of protein BF1032 from Bacteroides fragilis, Northeast Structural… · 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 Q64XJ4
Elsewhere: RCSB PDB 3NRH · PDBe 3NRH · UniProt Q64XJ4

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