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Crystal structure of calcium-bound D,D-heptose 1.7-bisphosphate phosphatase from E. COLI

Analyse Crystal structure of calcium-bound D,D-heptose 1.7-bisphosphate phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ESQ
Type: protein
Length: 182 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D,D-heptose 1,7-bisphosphate phosphatase
EC: 3.1.3.-
UniProt: P63228
Ligands: ZN, CA
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D,D-heptose 1,7-bisphosphate phosphatase (EC 3.1.3.-)	protein	182	40% helix, 19% strand	P63228

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CA · Calcium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	98	0.50	0.83	20	CA

Compared structures

3ESQ · Crystal Structure of Calcium-bound D,D-heptose 1.7-bisphosphate phosphatase from E. Coli · the same entry in another collection · chain A against A, TM-score 1.00
P63228 · AlphaFold monomer V2.0 prediction for D-glycero-beta-D-manno- heptose-1,7-bisphosphate… · 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 P63228
Elsewhere: RCSB PDB 3ESQ · PDBe 3ESQ · UniProt P63228

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