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Crystal structure of apo pullulanase from klebsiella pneumoniae in space group P43212

Analyse Crystal structure of apo pullulanase from klebsiella pneumoniae in space group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YN2
Type: protein
Length: 1,054 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pula protein
UniProt: W9BQ28
Ligands: CA, MG
Pockets: 7 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pula protein	protein	1054	28% helix, 23% strand	W9BQ28

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A
MG · Magnesium ion · metal · 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	449	0.65	0.78	44	empty
2	203	0.62	0.82	36	empty
3	173	0.48	0.77	25	empty
4	160	0.47	0.76	25	empty
5	103	0.40	0.76	17	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

5YN2 · Crystal structure of apo Pullulanase from Klebsiella pneumoniae in space group P43212 · 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 5YN2 · PDBe 5YN2 · UniProt W9BQ28

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