MolNFT v1 · #114056 · protein

Structure of the flih-flii complex

5B0O · Flagellum-specific ATP synthase: “Structure of the flih-flii complex”. X-ray diffraction, 1 ligand (ADP), 20 pockets (best druggability 0.86). MolNFT v1 #114056 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5B0O
Type: protein
Length: 2,858 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellum-specific ATP synthase; Flagellar assembly protein flih
EC: 3.6.3.14
UniProt: P26465, P15934
Ligands: ADP
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 9 distinct chains · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellum-specific ATP synthase (EC 3.6.3.14)	protein	445	38% helix, 22% strand	P26465
B	Flagellum-specific ATP synthase (EC 3.6.3.14)	protein	455	38% helix, 22% strand	P26465
C	Flagellum-specific ATP synthase (EC 3.6.3.14)	protein	445	39% helix, 22% strand	P26465
D	Flagellum-specific ATP synthase (EC 3.6.3.14)	protein	454	38% helix, 23% strand	P26465
E	Flagellar assembly protein flih	protein	135	61% helix, 10% strand	P15934
F	Flagellar assembly protein flih	protein	126	54% helix, 10% strand	P15934
G, H	Flagellar assembly protein flih	protein	136	58% helix, 10% strand	P15934
I, J, K	Flagellar assembly protein flih	protein	133	63% helix, 11% strand	P15934
L	Flagellar assembly protein flih	protein	127	59% helix, 9% strand	P15934

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	930	0.86	0.87	103	empty
2	776	0.85	0.88	82	empty
3	754	0.79	0.83	94	ADP
4	970	0.77	0.79	86	empty
5	888	0.75	0.79	81	empty

Interfaces

21 interfaces between chains.

H–L · 2507 Å² buried · 16 hydrogen bonds · protein-protein
F–J · 2167 Å² buried · 12 hydrogen bonds · protein-protein
G–K · 1871 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 1860 Å² buried · 22 hydrogen bonds · protein-protein
E–I · 1787 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5B0O · Structure of the FliH-FliI complex · the same entry in another collection · chain L against L, 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 P26465
Every structure of UniProt P15934
Elsewhere: RCSB PDB 5B0O · PDBe 5B0O · UniProt P26465 · UniProt P15934

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