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NMR structure of protein Hydrogenase-1 operon protein hyaE from Escherichia coli: Northeast Structural Genomics Consortium Target ER415

Analyse NMR structure of protein Hydrogenase-1 operon protein hyaE from Escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HFD
Type: protein
Length: 132 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: NOT
Source: Escherichia coli
Molecule: Hydrogenase-1 operon protein hyaE
UniProt: P19931
Pockets: 2 · best druggability 0.71

Structure

solution nmr · resolution NOT · 1 distinct chain · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydrogenase-1 operon protein hyaE	protein	132	38% helix, 20% strand	P19931

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	362	0.71	0.83	41	empty
2	54	0.42	0.82	17	empty

Compared structures

2HFD · NMR structure of protein hydrogenase-1 operon protein hyae from escherichia COLI… · the same entry in another collection · chain A against A, TM-score 1.00
P19931 · AlphaFold monomer V2.0 prediction for hydrogenase-1 operon protein hyae (P19931) · a predicted model of the same protein · chain A against A, TM-score 0.78

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 P19931
Elsewhere: RCSB PDB 2HFD · PDBe 2HFD · UniProt P19931

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