MolNFT v1 · #154559 · protein

Hydroxynitrile lyase from the millipede, chamberlinius hualienensis bound with acetate

6KFA: “Hydroxynitrile lyase from the millipede, chamberlinius hualienensis bound with acetate”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.59). MolNFT v1 #154559 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6KFA
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: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydroxynitrile lyase	protein	162	15% helix, 40% strand	A0A0H5BR52

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.59	0.88	22	ACT

Modifications

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

Compared structures

6KFA · Hydroxynitrile lyase from the millipede, Chamberlinius hualienensis bound with acetate · 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 6KFA · PDBe 6KFA · UniProt A0A0H5BR52

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