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Crystal structure of xenotropic murine leukemia virus-related virus (xmrv) protease

Analyse Crystal structure of xenotropic murine leukemia virus-related virus (xmrv)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NR6
Type: protein
Length: 234 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease P14
EC: 3.4.23.-
UniProt: A1Z651
Ligands: K, PO4
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protease P14 (EC 3.4.23.-)	protein	120	8% helix, 43% strand	A1Z651
B	Protease P14 (EC 3.4.23.-)	protein	114	6% helix, 46% strand	A1Z651

Ligands and binding sites

K · Potassium ion · metal · chains A
PO4 · Phosphate 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	299	0.53	0.74	36	empty

Interfaces

1 interface between chains.

A–B · 823 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3NR6 · Crystal structure of xenotropic murine leukemia virus-related virus (XMRV) protease · 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 A1Z651
Elsewhere: RCSB PDB 3NR6 · PDBe 3NR6 · UniProt A1Z651

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