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The crystal structure of pvuii endonuclease reveals extensive structural homologies to ecorv

Analyse The crystal structure of pvuii endonuclease reveals extensive structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PVU
Type: protein
Length: 308 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pvu II
EC: 3.1.21.4
UniProt: P23657
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pvu II (EC 3.1.21.4)	protein	154	42% helix, 23% strand	P23657

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	100	0.36	0.74	15	empty
2	97	0.34	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 1609 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

1PVU · The crystal structure of pvuii endonuclease reveals extensive structural homologies to… · the same entry in another collection · chain A against A, TM-score 1.00
P23657 · AlphaFold monomer V2.0 prediction for type-2 restriction enzyme pvuii (P23657) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P23657
Elsewhere: RCSB PDB 1PVU · PDBe 1PVU · UniProt P23657

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