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Solution structure of the chimeric AF1503 hamp- envz dhp homodimer

Analyse Solution structure of the chimeric AF1503 hamp- envz dhp homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LFR
Type: protein
Length: 222 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hamp domain-containing protein, osmolarity sensor protein enzv chimera
EC: 2.7.13.3
UniProt: O28769, P0AEJ5
Pockets: 1 · best druggability 0.79

Structure

solution nmr · 1 distinct chain · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hamp domain-containing protein, osmolarity sensor protein enzv chimera (EC 2.7.13.3)	protein	111	80% helix, 0% strand	O28769, P0AEJ5

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	279	0.79	0.90	38	empty

Interfaces

1 interface between chains.

A–B · 2159 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

2LFR · Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer · the same entry in another collection · chain A against A, TM-score 1.00
P0AEJ5 · AlphaFold monomer V2.0 prediction for sensor histidine kinase envz (P0AEJ5) · a predicted model of the same protein · chain B against A, TM-score 0.80

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 O28769
Every structure of UniProt P0AEJ5
Elsewhere: RCSB PDB 2LFR · PDBe 2LFR · UniProt O28769 · UniProt P0AEJ5

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