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E. COLI ribonuclease hi in complex one ZN2+ (HIS124 N-epsilon binding)

Analyse E. COLI ribonuclease hi in complex one ZN2+ (HIS124 N-epsilon binding) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7VSE
Type: protein
Length: 310 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease hi
EC: 3.1.26.4
UniProt: P0A7Y4
Ligands: ZN, SO4
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonuclease hi (EC 3.1.26.4)	protein	155	36% helix, 32% strand	P0A7Y4

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 4 copies · chains A, B
GOL · Glycerol · additive · chains B

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

Pockets

3 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	669	0.69	0.77	62	SO4
2	52	0.34	0.78	13	empty
3	64	0.32	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 665 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7VSE · E. coli Ribonuclease HI in complex one Zn2+ (His124 N-epsilon binding) · 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 P0A7Y4
Elsewhere: RCSB PDB 7VSE · PDBe 7VSE · UniProt P0A7Y4

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