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Athnl enantioselectivity mutant at-A9-H7 apo Y13C,Y121L,P126F,L128W, C131T,F179L,A209I with benzaldehyde, mandelic acid nitrile

Analyse Athnl enantioselectivity mutant at-A9-H7 apo Y13C,Y121L,P126F,L128W… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6COE
Type: protein
Length: 517 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9LFT6
Ligands: HBX, MNN, MXN, CL

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	258	—	Q9LFT6
B	—	protein	259	—	Q9LFT6

Ligands and binding sites

HBX · benzaldehyde · ligand · 2 copies · chains A
MNN · (S)-mandelic acid nitrile · ligand · 2 copies · chains A, B
MXN · (2R)-hydroxy(phenyl)ethanenitrile · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · 4 copies · chains A, B

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

Compared structures

6COE · AtHNL enantioselectivity mutant At-A9-H7 Apo Y13C,Y121L,P126F,L128W,C131T,F179L,A209I… · the same entry in another collection · chain A against A, TM-score 1.00
Q9LFT6 · AlphaFold monomer V2.0 prediction for alpha-hydroxynitrile lyase (Q9LFT6) · a predicted model of the same protein · 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 Q9LFT6
Elsewhere: RCSB PDB 6COE · PDBe 6COE · UniProt Q9LFT6

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