MolNFT v1 · #36801 · protein

Crystal structure analysis of apo pullulanase from klebsiella pneumoniae

2FGZ · Alpha-dextrin endo-1,6-alpha-glucosidase: “Crystal structure analysis of apo pullulanase from klebsiella pneumoniae”. X-ray diffraction, 1 ligand (CA), 7 pockets (best druggability 0.62). MolNFT v1 #36801 on GenesisL1: 3D structure…

PDB: 2FGZ
Type: protein
Length: 926 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-dextrin endo-1,6-alpha-glucosidase
EC: 3.2.1.41
UniProt: W9BQ28
Ligands: CA
Pockets: 7 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-dextrin endo-1,6-alpha-glucosidase (EC 3.2.1.41)	protein	926	30% helix, 22% strand	W9BQ28

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	251	0.62	0.81	40	empty
2	403	0.61	0.76	36	empty
3	165	0.49	0.78	29	empty
4	132	0.42	0.76	20	empty
5	89	0.37	0.76	18	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2FGZ · Crystal Structure Analysis of apo pullulanase from Klebsiella pneumoniae · 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 W9BQ28
Elsewhere: RCSB PDB 2FGZ · PDBe 2FGZ · UniProt W9BQ28

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