MolNFT v2 · #213797 · protein

Reductive aminase RA29-WT

8J43 · Beta-hydroxyacid dehydrogenase, 3-hydroxyisobutyrate…: “Reductive aminase RA29-WT”. X-ray diffraction at 2.03, 1 ligand (NAP), 2 pockets (best druggability 0.77). MolNFT v2 #213797 on GenesisL1: 3D structure, binding sites and…

PDB: 8J43
Type: protein
Length: 570 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.03
Source: Frankia sp. QA3
Molecule: Beta-hydroxyacid dehydrogenase, 3-hydroxyisobutyrate dehydrogenase
UniProt: I8QLV7
Ligands: NAP
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · resolution 2.03 · 1 distinct chain · 59% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-hydroxyacid dehydrogenase, 3-hydroxyisobutyrate dehydrogenase	protein	285	59% helix, 13% strand	I8QLV7

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

2 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	365	0.77	0.87	43	EDO, NAP
2	355	0.76	0.87	43	NAP, EDO

Interfaces

1 interface between chains.

A–B · 4520 Å² buried · 28 hydrogen bonds · protein-protein

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 I8QLV7
Elsewhere: RCSB PDB 8J43 · PDBe 8J43 · UniProt I8QLV7

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