MolNFT v1 · #151895 · protein

Crystal structure of rutinosidase from aspergillus niger

6I1A: “Crystal structure of rutinosidase from aspergillus niger”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.86). MolNFT v1 #151895 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6I1A
Type: protein
Length: 716 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rutinosidase
UniProt: A0A254TQT9
Ligands: NAG
Pockets: 1 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Rutinosidase	protein	358	42% helix, 15% strand	A0A254TQT9

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
EDO · 1,2-ethanediol · additive · 28 copies · chains A, B

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	1187	0.86	0.87	118	EDO

Interfaces

1 interface between chains.

A–B · 784 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 glycan, 2 disulfide (N-glycosylation, disulfide).

Compared structures

6I1A · Crystal structure of rutinosidase from Aspergillus niger · 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 A0A254TQT9
Elsewhere: RCSB PDB 6I1A · PDBe 6I1A · UniProt A0A254TQT9

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