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Crystal structure of BFA1

Analyse Crystal structure of BFA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YVF
Type: protein
Length: 1,270 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BFA1
UniProt: A0A178VCD5
Pockets: 11 · best druggability 0.83

Structure

x-ray diffraction · 4 distinct chains · 15% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BFA1	protein	322	15% helix, 52% strand	A0A178VCD5
B	BFA1	protein	312	15% helix, 54% strand	A0A178VCD5
C	BFA1	protein	318	15% helix, 54% strand	A0A178VCD5
D	BFA1	protein	318	15% helix, 53% strand	A0A178VCD5

Pockets

11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1156	0.83	0.84	109	empty
2	105	0.64	0.89	24	empty
3	109	0.63	0.88	24	empty
4	329	0.62	0.78	46	empty
5	236	0.58	0.79	35	empty

Interfaces

5 interfaces between chains.

A–B · 1089 Å² buried · 9 hydrogen bonds · protein-protein
B–D · 248 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 113 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 21 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 20 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5YVF · Crystal structure of BFA1 · the same entry in another collection · chain C against C, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A178VCD5
Elsewhere: RCSB PDB 5YVF · PDBe 5YVF · UniProt A0A178VCD5

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