MolNFT v1 · #5289 · protein

Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions: studies with halide compounds reveal a halide binding site in the active site

1EDD: “Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions…”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.36). MolNFT v1 #5289 on GenesisL1: 3D structure, binding…

PDB: 1EDD
Type: protein
Length: 310 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Haloalkane dehalogenase
EC: 3.8.1.5
UniProt: P22643
Ligands: CL
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Haloalkane dehalogenase (EC 3.8.1.5)	protein	310	43% helix, 14% strand	P22643

Ligands and binding sites

CL · Chloride ion · ion · 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	54	0.36	0.79	15	empty

Compared structures

1EDD · Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase… · the same entry in another collection · chain A against A, TM-score 1.00
P22643 · AlphaFold monomer V2.0 prediction for haloalkane dehalogenase (P22643) · 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 P22643
Elsewhere: RCSB PDB 1EDD · PDBe 1EDD · UniProt P22643

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