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Crystal structure of apo pullulanase from paenibacillus barengoltzii

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

PDB: 6JHF
Type: protein
Length: 653 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: CA, CL
Pockets: 5 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pulullanase (EC 3.2.1.41)	protein	653	31% helix, 23% strand	A0A0C5GWS2

Ligands and binding sites

CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	311	0.59	0.77	36	empty
2	192	0.50	0.76	22	empty
3	100	0.42	0.78	22	empty
4	75	0.38	0.78	18	empty
5	98	0.38	0.76	19	empty

Compared structures

6JHF · Crystal structure of apo 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 6JHF · PDBe 6JHF · UniProt A0A0C5GWS2

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