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Crystal structure of fragment 1600-1733 of HSV1 UL36, native

Analyse Crystal structure of fragment 1600-1733 of HSV1 UL36, native in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TT1
Type: protein
Length: 253 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.75
Source: Herpes simplex virus (type 1 / strain 17)
Molecule: Deneddylase
EC: 3.4.19.12, 3.4.22.-
UniProt: P10220
Ligands: PO4
Pockets: 2 · best druggability 0.33

Structure

x-ray diffraction · resolution 2.75 · 2 distinct chains · 76% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deneddylase (EC 3.4.19.12, 3.4.22.-)	protein	124	76% helix, 0% strand	P10220
B	Deneddylase (EC 3.4.19.12, 3.4.22.-)	protein	129	77% helix, 2% strand	P10220

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains B

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

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	64	0.33	0.76	12	empty
2	58	0.30	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 2300 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

4TT1 · Crystal structure of fragment 1600-1733 of HSV1 UL36, native · 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 P10220
Elsewhere: RCSB PDB 4TT1 · PDBe 4TT1 · UniProt P10220

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