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Crystal structure of escherichia COLI phytase at pH 6.6 with HG2+ cation acting as an intermolecular bridge

Analyse Crystal structure of escherichia COLI phytase at pH 6.6 with HG2+ cation acting… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DKM
Type: protein
Length: 410 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phytase
EC: 3.1.3.2
UniProt: P07102
Ligands: HG
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phytase (EC 3.1.3.2)	protein	410	41% helix, 17% strand	P07102

Ligands and binding sites

HG · Mercury (II) ion · metal · chains A

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

Pockets

2 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	437	0.62	0.77	49	empty
2	51	0.31	0.77	13	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1DKM · Crystal structure of escherichia COLI phytase at pH 6.6 with HG2+ cation acting as an… · the same entry in another collection · chain A against A, TM-score 1.00
P07102 · AlphaFold monomer V2.0 prediction for periplasmic appa protein (P07102) · 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 P07102
Elsewhere: RCSB PDB 1DKM · PDBe 1DKM · UniProt P07102

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