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Crystal structure of B. halodurans RNase H catalytic domain mutant D132N

Analyse Crystal structure of B. halodurans RNase H catalytic domain mutant D132N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZBF
Type: protein
Length: 132 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease H-related protein
EC: 3.1.26.4
UniProt: Q9KEI9
Ligands: SO4
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonuclease H-related protein (EC 3.1.26.4)	protein	132	36% helix, 23% strand	Q9KEI9

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.33	0.77	12	empty

Compared structures

1ZBF · Crystal structure of B. halodurans RNase H catalytic domain mutant D132N · the same entry in another collection · chain A against A, TM-score 1.00
Q9KEI9 · AlphaFold monomer V2.0 prediction for ribonuclease H (Q9KEI9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9KEI9
Elsewhere: RCSB PDB 1ZBF · PDBe 1ZBF · UniProt Q9KEI9

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