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Crystal structure of fragment 1600-1733 of HSV1 UL36 in the presence of 1M potassium iodide

Analyse Crystal structure of fragment 1600-1733 of HSV1 UL36 in the presence of 1M… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TT0
Type: protein
Length: 260 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deneddylase
EC: 3.4.19.12, 3.4.22.-
UniProt: P10220
Ligands: IOD
Pockets: 2 · best druggability 0.33

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deneddylase (EC 3.4.19.12, 3.4.22.-)	protein	129	74% helix, 2% strand	P10220
B	Deneddylase (EC 3.4.19.12, 3.4.22.-)	protein	131	76% helix, 2% strand	P10220

Ligands and binding sites

IOD · Iodide ion · ion · 40 copies · chains A, 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	70	0.33	0.75	13	IOD
2	53	0.30	0.76	12	empty

Interfaces

1 interface between chains.

A–B · 2390 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

4TT0 · Crystal structure of fragment 1600-1733 of HSV1 UL36 in the presence of 1M potassium… · 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 4TT0 · PDBe 4TT0 · UniProt P10220

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