Research workbench

Crystal structure of the fluoroacetate dehalogenase RPA1163 - TYR219PHE - apo

Analyse Crystal structure of the fluoroacetate dehalogenase RPA1163 - TYR219PHE - apo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6QKS
Type: protein
Length: 600 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fluoroacetate dehalogenase
UniProt: A0A2R4GQN1
Ligands: CL
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fluoroacetate dehalogenase	protein	303	46% helix, 16% strand	A0A2R4GQN1
B	Fluoroacetate dehalogenase	protein	297	45% helix, 16% strand	A0A2R4GQN1

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	138	0.41	0.74	23	empty
2	75	0.34	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 1202 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

6QKS · Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Tyr219Phe - Apo · the same entry in another collection · 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 A0A2R4GQN1
Elsewhere: RCSB PDB 6QKS · PDBe 6QKS · UniProt A0A2R4GQN1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.