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Structure of pffnt in apo state

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

PDB: 7E26
Type: protein
Length: 1,435 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Formate-nitrite transporter
UniProt: O77389
Pockets: 20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D, A, B, C, E	Formate-nitrite transporter	protein	287	75% helix, 1% strand	O77389

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1022	0.88	0.87	63	empty
2	107	0.76	0.96	25	empty
3	409	0.74	0.84	42	empty
4	73	0.73	0.97	21	empty
5	476	0.72	0.81	45	empty

Interfaces

10 interfaces between chains.

D–E · 2121 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 2109 Å² buried · 13 hydrogen bonds · protein-protein
A–E · 2107 Å² buried · 13 hydrogen bonds · protein-protein
D–C · 2100 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 2094 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7E26 · Structure of PfFNT in apo state · the same entry in another collection · chain D against D, 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 O77389
Elsewhere: RCSB PDB 7E26 · PDBe 7E26 · UniProt O77389

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