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Crystal structures of bacillus subtilis alkaline phytase in complex with CA2+, CO2+, NI2+, MG2+ and myo-inositol hexasulfate

Analyse Crystal structures of bacillus subtilis alkaline phytase in complex with CA2+… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AMR
Type: protein
Length: 352 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-phytase
EC: 3.1.3.8
UniProt: O31097
Ligands: IHS, CA
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-phytase (EC 3.1.3.8)	protein	352	6% helix, 48% strand	O31097

Ligands and binding sites

IHS · D-myo-inositol-hexasulphate · ligand · chains A
CA · Calcium ion · metal · 11 copies · chains A

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	207	0.81	0.95	44	CA

Compared structures

3AMR · Crystal Structures of Bacillus subtilis Alkaline Phytase in Complex with Ca2+, Co2+… · the same entry in another collection · chain A against A, TM-score 1.00
O31097 · AlphaFold monomer V2.0 prediction for 3-phytase (O31097) · a predicted model of the same protein · 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 O31097
Elsewhere: RCSB PDB 3AMR · PDBe 3AMR · UniProt O31097

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