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Crystal structure of S-nitrosoglutathione reductase apoenzyme from tomato (solanum lycopersicum)

Analyse Crystal structure of S-nitrosoglutathione reductase apoenzyme from tomato… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DLA
Type: protein
Length: 758 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alcohol dehydrogenase class III
EC: 1.1.1.1
UniProt: D2Y3F4
Ligands: ZN
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alcohol dehydrogenase class III (EC 1.1.1.1)	protein	379	31% helix, 26% strand	D2Y3F4

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B
GOL · Glycerol · additive · 10 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1058	0.79	0.80	90	GOL
2	1126	0.78	0.79	86	GOL
3	495	0.66	0.78	60	empty

Interfaces

1 interface between chains.

A–B · 1624 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

4DLA · Crystal structure of S-nitrosoglutathione reductase apoenzyme from tomato (Solanum… · 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 D2Y3F4
Elsewhere: RCSB PDB 4DLA · PDBe 4DLA · UniProt D2Y3F4

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