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Solution structure of hndac : a thioredoxin-like [2FE-2S] ferredoxin involved in the NADP-reducing hydrogenase complex

Analyse Solution structure of hndac : a thioredoxin-like [2FE-2S] ferredoxin involved… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AUV
Type: protein
Length: 85 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potential NAD-reducing hydrogenase subunit
EC: 1.12.1.3
UniProt: Q46505
Ligands: FES
Pockets: 1 · best druggability 0.47

Structure

solution nmr · 1 distinct chain · 35% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Potential NAD-reducing hydrogenase subunit (EC 1.12.1.3)	protein	85	35% helix, 8% strand	Q46505

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	132	0.47	0.78	23	FES

Compared structures

2AUV · Solution Structure of HndAc : A Thioredoxin-like [2Fe-2S] Ferredoxin Involved in the… · the same entry in another collection · chain A against A, TM-score 1.00
Q46505 · AlphaFold monomer V2.0 prediction for NADP-reducing hydrogenase subunit hnda (Q46505) · a predicted model of the same protein · chain A against A, TM-score 0.63

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 Q46505
Elsewhere: RCSB PDB 2AUV · PDBe 2AUV · UniProt Q46505

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