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Crystal structure of D-allose kinase (NP_418508.1) from escherichia COLI K12 at 1.95 a resolution

Analyse Crystal structure of D-allose kinase (NP_418508.1) from escherichia COLI K12 at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HTV
Type: protein
Length: 279 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-allose kinase
EC: 2.7.1.55
UniProt: P32718
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-allose kinase (EC 2.7.1.55)	protein	279	38% helix, 24% strand	P32718

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	472	0.61	0.76	47	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

3HTV · Crystal structure of D-allose kinase (NP_418508.1) from ESCHERICHIA COLI K12 at 1.95 A… · the same entry in another collection · chain A against A, TM-score 1.00
P32718 · AlphaFold monomer V2.0 prediction for D-allose kinase (P32718) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P32718
Elsewhere: RCSB PDB 3HTV · PDBe 3HTV · UniProt P32718

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