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Structure of rhodococcus rhodochrous haloalkane dehalogenase dhaa mutant DHAA12

Analyse Structure of rhodococcus rhodochrous haloalkane dehalogenase dhaa mutant DHAA12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SK0
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Haloalkane dehalogenase
EC: 3.8.1.5
UniProt: P0A3G2
Ligands: CL
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Haloalkane dehalogenase (EC 3.8.1.5)	protein	308	46% helix, 19% strand	P0A3G2

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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	179	0.61	0.83	30	CL

Compared structures

3SK0 · structure of Rhodococcus rhodochrous haloalkane dehalogenase DhaA mutant DhaA12 · the same entry in another collection · chain A against A, TM-score 1.00
P0A3G2 · AlphaFold monomer V2.0 prediction for haloalkane dehalogenase (P0A3G2) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P0A3G2
Elsewhere: RCSB PDB 3SK0 · PDBe 3SK0 · UniProt P0A3G2

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