MolNFT v1 · #141098 · protein

Structure-guided engineering of reductase: efficient attenuating substrate inhibition in asymmetric catalysis

5YW4 · Protein induced by osmotic stress: “Structure-guided engineering of reductase: efficient attenuating substrate inhibition in asymmetric catalysis”. X-ray diffraction, 1 ligand (NAP), 3 pockets (best druggability 0.75). MolNFT v1…

PDB: 5YW4
Type: protein
Length: 331 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein induced by osmotic stress
EC: 1.1.1.195
UniProt: A3LWG4
Ligands: NAP
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein induced by osmotic stress (EC 1.1.1.195)	protein	331	46% helix, 15% strand	A3LWG4

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	612	0.75	0.82	61	NAP
2	75	0.58	0.88	20	empty
3	67	0.39	0.79	12	empty

Compared structures

5YW4 · Structure-Guided Engineering of Reductase: Efficient Attenuating Substrate Inhibition in… · 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 A3LWG4
Elsewhere: RCSB PDB 5YW4 · PDBe 5YW4 · UniProt A3LWG4

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