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Imine reductase from amycolatopsis orientalis in complex with (R)-methyltetrahydroisoquinoline

Analyse Imine reductase from amycolatopsis orientalis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A9T
Type: protein
Length: 286 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative dehydrogenase
EC: 1.5.1.48
UniProt: R4SNK4
Ligands: YLG, CA
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative dehydrogenase (EC 1.5.1.48)	protein	286	55% helix, 14% strand	R4SNK4

Ligands and binding sites

YLG · (1R)-1-methyl-1,2,3,4-tetrahydroisoquinoline · ligand · chains A
CA · Calcium ion · metal · chains A
ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	493	0.59	0.73	38	empty
2	93	0.46	0.81	18	empty
3	94	0.35	0.74	21	empty

Compared structures

5A9T · Imine Reductase from Amycolatopsis orientalis in complex with (R)… · 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 R4SNK4
Elsewhere: RCSB PDB 5A9T · PDBe 5A9T · UniProt R4SNK4

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