MolNFT v1 · #25251 · protein

Conserved hypothetical protein from pyrococcus furiosus pfu-392566-001

1VK1: “Conserved hypothetical protein from pyrococcus furiosus pfu-392566-001”. X-ray diffraction, 2 ligands (NA, PO4), 2 pockets (best druggability 0.57). MolNFT v1 #25251 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1VK1
Type: protein
Length: 232 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Conserved hypothetical protein
UniProt: Q8U3S5
Ligands: NA, PO4
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Conserved hypothetical protein	protein	232	35% helix, 27% strand	Q8U3S5

Ligands and binding sites

NA · Sodium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

2 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	268	0.57	0.77	32	PO4, NA
2	95	0.39	0.77	17	PEG

Modifications

Observed in the structure: 9 modified (methylation).

Compared structures

1VK1 · Conserved hypothetical protein from Pyrococcus furiosus Pfu-392566-001 · 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 Q8U3S5
Elsewhere: RCSB PDB 1VK1 · PDBe 1VK1 · UniProt Q8U3S5

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