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Crystal structure of poplar glutathione transferase F1 mutant ser 13 cys

Analyse Crystal structure of poplar glutathione transferase F1 mutant ser 13 cys in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4RI7
Type
protein
Length
428 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phi class glutathione transferase GSTF1
EC
2.5.1.18
UniProt
A9PHH6
Ligands
GSH
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPhi class glutathione transferase GSTF1 (EC 2.5.1.18)protein21458% helix, 7% strandA9PHH6

Ligands and binding sites

  • GSH · Glutathione · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110010.770.7978GSH
2920.590.8728empty
3670.380.7918empty
4600.270.7315empty
5500.260.7419empty

Interfaces

1 interface between chains.

  • A–B · 1463 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 4RI7 · Crystal structure of poplar glutathione transferase F1 mutant SER 13 CYS · the same entry in another collection · chain B against B, TM-score 1.00

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