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Viral chemokine binding protein R17 encoded by rodent gammaherpesvirus peru ( rhvp)

Analyse Viral chemokine binding protein R17 encoded by rodent gammaherpesvirus peru (… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZKQ
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein
UniProt: E9M5R0
Ligands: NAG
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein	protein	388	5% helix, 47% strand	E9M5R0

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

4 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	290	0.61	0.79	32	empty
2	66	0.41	0.80	18	empty
3	56	0.35	0.78	19	empty
4	60	0.31	0.75	14	empty

Modifications

Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

4ZKQ · Viral chemokine binding protein R17 encoded by rodent gammaherpesvirus Peru ( RHVP) · 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 E9M5R0
Elsewhere: RCSB PDB 4ZKQ · PDBe 4ZKQ · UniProt E9M5R0

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