MolNFT v1 · #101993 · protein

Structure of the H170Y mutant of thermostable P-nitrophenylphosphatase from bacillus stearothermophilus

4O8C · Thermostable nppase: “Structure of the H170Y mutant of thermostable P-nitrophenylphosphatase from bacillus stearothermophilus”. X-ray diffraction, 2 ligands (MG, SO4), 4 pockets (best druggability 0.69). MolNFT v1 #101993 on…

PDB: 4O8C
Type: protein
Length: 510 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thermostable nppase
EC: 3.1.3.1
UniProt: Q8L1N9
Ligands: MG, SO4
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thermostable nppase (EC 3.1.3.1)	protein	255	42% helix, 20% strand	Q8L1N9

Ligands and binding sites

MG · Magnesium ion · metal · chains B
SO4 · Sulfate ion · ion · chains B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	468	0.69	0.80	54	MG, SO4
2	291	0.54	0.75	37	empty
3	93	0.43	0.79	21	empty
4	52	0.34	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 1271 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

4O8C · Structure of the H170Y mutant of thermostable p-nitrophenylphosphatase from Bacillus… · 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 Q8L1N9
Elsewhere: RCSB PDB 4O8C · PDBe 4O8C · UniProt Q8L1N9

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