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Crystal structure of R-protein of ngoavii restriction endonuclease

Analyse Crystal structure of R-protein of ngoavii restriction endonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RCT
Type: protein
Length: 694 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Restriction endonuclease R.NGOVII
EC: 3.1.21.4
UniProt: Q5F9M9
Pockets: 6 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Restriction endonuclease R.NGOVII (EC 3.1.21.4)	protein	347	31% helix, 25% strand	Q5F9M9

Pockets

6 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	1006	0.84	0.85	93	empty
2	164	0.42	0.73	28	empty
3	79	0.31	0.74	17	empty
4	62	0.30	0.75	17	empty
5	62	0.29	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 1629 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (artifact).

Compared structures

4RCT · Crystal structure of R-protein of NgoAVII restriction endonuclease · 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 Q5F9M9
Elsewhere: RCSB PDB 4RCT · PDBe 4RCT · UniProt Q5F9M9

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