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Crystal structure of flhd from escherichia COLI

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

PDB: 1G8E
Type: protein
Length: 178 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar transcriptional activator flhd
UniProt: P0A8S9
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 69% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar transcriptional activator flhd	protein	98	69% helix, 3% strand	P0A8S9
B	Flagellar transcriptional activator flhd	protein	80	68% helix, 4% strand	P0A8S9

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	84	0.31	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 2581 Å² buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1G8E · Crystal structure of flhd from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
P0A8S9 · AlphaFold monomer V2.0 prediction for flagellar transcriptional regulator flhd (P0A8S9) · a predicted model of the same protein · chain B against A, TM-score 0.91

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 P0A8S9
Elsewhere: RCSB PDB 1G8E · PDBe 1G8E · UniProt P0A8S9

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