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Cadmium inhibited crystal structure of phytase from bacillus amyloliquefaciens

Analyse Cadmium inhibited crystal structure of phytase from bacillus amyloliquefaciens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CVM
Type: protein
Length: 353 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phytase
EC: 3.1.3.8
UniProt: O66037
Ligands: CD, CA
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phytase (EC 3.1.3.8)	protein	353	5% helix, 47% strand	O66037

Ligands and binding sites

CD · Cadmium ion · metal · 5 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

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	229	0.82	0.95	45	CA

Compared structures

1CVM · Cadmium inhibited crystal structure of phytase from bacillus amyloliquefaciens · the same entry in another collection · chain A against A, TM-score 1.00
O66037 · AlphaFold monomer V2.0 prediction for 3-phytase (O66037) · 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 O66037
Elsewhere: RCSB PDB 1CVM · PDBe 1CVM · UniProt O66037

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