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Crystal structure of the fluoroacetate dehalogenase RPA1163 - TYR219PHE - fluoroacetate soaked 24HR - glycolate bound

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

PDB: 6QKT
Type: protein
Length: 591 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fluoroacetate dehalogenase
UniProt: A0A2R4GQN1
Ligands: GOA
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fluoroacetate dehalogenase	protein	297	46% helix, 16% strand	A0A2R4GQN1
B	Fluoroacetate dehalogenase	protein	294	46% helix, 17% strand	A0A2R4GQN1

Ligands and binding sites

GOA · Glycolic acid · ligand · chains A

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	140	0.46	0.77	28	empty
2	100	0.38	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 1181 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6QKT · Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Tyr219Phe - Fluoroacetate… · 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 6QKT · PDBe 6QKT · UniProt A0A2R4GQN1

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