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Crystal structure of mutant D350A of pullulanase from paenibacillus barengoltzii complexed with maltotriose

Analyse Crystal structure of mutant D350A of pullulanase from paenibacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JHH
Type: protein
Length: 642 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pulullanase
EC: 3.2.1.41
UniProt: A0A0C5GWS2
Ligands: GLC, CA
Pockets: 7 · best druggability 0.60

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pulullanase (EC 3.2.1.41)	protein	642	30% helix, 22% strand	A0A0C5GWS2

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 9 copies · chains A
CA · Calcium ion · metal · 3 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	286	0.60	0.78	33	GLC
2	207	0.54	0.78	30	empty
3	99	0.42	0.78	18	empty
4	91	0.41	0.78	20	empty
5	72	0.34	0.76	13	empty

Compared structures

6JHH · Crystal structure of mutant D350A of Pullulanase from Paenibacillus barengoltzii… · 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 A0A0C5GWS2
Elsewhere: RCSB PDB 6JHH · PDBe 6JHH · UniProt A0A0C5GWS2

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