MolNFT v1 · #120609 · protein

Crystal structure of the flagellar cap protein flid D1-D2-D3 domains from escherichia COLI

5H5V · Flagellar hook-associated protein 2: “Crystal structure of the flagellar cap protein flid D1-D2-D3 domains from escherichia COLI”. X-ray diffraction, 11 pockets (best druggability 0.69). MolNFT v1 #120609 on GenesisL1: 3D structure…

PDB: 5H5V
Type: protein
Length: 2,021 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar hook-associated protein 2
UniProt: A0A094VPA5
Pockets: 11 · best druggability 0.69

Structure

x-ray diffraction · 6 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar hook-associated protein 2	protein	352	38% helix, 26% strand	A0A094VPA5
B	Flagellar hook-associated protein 2	protein	339	35% helix, 27% strand	A0A094VPA5
C	Flagellar hook-associated protein 2	protein	356	37% helix, 25% strand	A0A094VPA5
D	Flagellar hook-associated protein 2	protein	345	36% helix, 27% strand	A0A094VPA5
E	Flagellar hook-associated protein 2	protein	299	34% helix, 28% strand	A0A094VPA5
F	Flagellar hook-associated protein 2	protein	330	35% helix, 28% strand	A0A094VPA5

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	577	0.69	0.78	76	empty
2	619	0.69	0.78	69	empty
3	597	0.69	0.78	74	empty
4	551	0.68	0.78	74	empty
5	474	0.66	0.78	66	empty

Interfaces

6 interfaces between chains.

D–E · 649 Å² buried · 7 hydrogen bonds · protein-protein
A–F · 648 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 624 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 616 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 551 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

5H5V · Crystal structure of the flagellar cap protein FliD D1-D2-D3 domains from Escherichia coli · 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 A0A094VPA5
Elsewhere: RCSB PDB 5H5V · PDBe 5H5V · UniProt A0A094VPA5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.