Research workbench

STM1697-flhd complex

Analyse STM1697-flhd complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HXG
Type: protein
Length: 552 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein STM1697; Flagellar transcriptional regulator flhd
UniProt: G4C3X3, G4C1X0
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Uncharacterized protein STM1697	protein	211	43% helix, 22% strand	G4C3X3
B, D	Flagellar transcriptional regulator flhd	protein	65	77% helix, 2% strand	G4C1X0

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	896	0.76	0.79	83	empty
2	233	0.51	0.75	33	empty
3	71	0.33	0.75	15	empty

Interfaces

3 interfaces between chains.

C–D · 1003 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 987 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 579 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

5HXG · STM1697-FlhD complex · 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 G4C3X3
Every structure of UniProt G4C1X0
Elsewhere: RCSB PDB 5HXG · PDBe 5HXG · UniProt G4C3X3 · UniProt G4C1X0

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