MolNFT v1 · #102581 · protein

5HMC specific restriction endonuclease PVURTS1I

4OQ2 · Restriction endonuclease PVURTS1 I: “5HMC specific restriction endonuclease PVURTS1I”. X-ray diffraction, 4 pockets (best druggability 0.79). MolNFT v1 #102581 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4OQ2
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Restriction endonuclease PVURTS1 I
EC: 3.1.21.-
UniProt: Q52612
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Restriction endonuclease PVURTS1 I (EC 3.1.21.-)	protein	297	29% helix, 29% strand	Q52612

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	718	0.79	0.83	62	empty
2	65	0.39	0.79	17	empty
3	120	0.38	0.74	16	empty
4	57	0.37	0.80	17	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

4OQ2 · 5hmC specific restriction endonuclease PvuRTs1I · 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 Q52612
Elsewhere: RCSB PDB 4OQ2 · PDBe 4OQ2 · UniProt Q52612

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