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Crystal structure of the F5/8 type C domain of Q5LFR2_BACFN protein from bacteroides fragilis. northeast structural genomics consortium target BFR258E

Analyse Crystal structure of the F5/8 type C domain of Q5LFR2_BACFN protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NNG
Type: protein
Length: 304 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q5LFR2
Ligands: CA
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	153	12% helix, 47% strand	Q5LFR2
B	Uncharacterized protein	protein	151	13% helix, 48% strand	Q5LFR2

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	246	0.54	0.77	39	empty
2	54	0.43	0.83	22	empty

Interfaces

1 interface between chains.

A–B · 807 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

3NNG · Crystal structure of the F5/8 type C domain of Q5LFR2_BACFN protein from Bacteroides… · 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 Q5LFR2
Elsewhere: RCSB PDB 3NNG · PDBe 3NNG · UniProt Q5LFR2

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