MolNFT v1 · #153531 · protein

Hydroxynitrile lyase from the millipede, chamberlinius hualienensis (ligand free)

6JHC: “Hydroxynitrile lyase from the millipede, chamberlinius hualienensis (ligand free)”. X-ray diffraction, 1 ligand (NAG), 2 pockets (best druggability 0.61). MolNFT v1 #153531 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6JHC
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydroxynitrile lyase
UniProt: A0A0H5BR52
Ligands: NAG
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydroxynitrile lyase	protein	162	15% helix, 41% strand	A0A0H5BR52

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

2 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	94	0.61	0.87	22	empty
2	52	0.39	0.81	14	empty

Modifications

Observed in the structure: 3 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

6JHC · Hydroxynitrile lyase from the millipede, Chamberlinius hualienensis (ligand free) · 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 A0A0H5BR52
Elsewhere: RCSB PDB 6JHC · PDBe 6JHC · UniProt A0A0H5BR52

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