MolNFT v1 · #73792 · protein

Structure of recombinant haemophilus influenzae E(P4) acid phosphatase mutant D66N complexed with nmn

3OCU · Lipoprotein E: “Structure of recombinant haemophilus influenzae E(P4) acid phosphatase mutant D66N complexed with nmn”. X-ray diffraction, 2 ligands (NMN, MG), 3 pockets (best druggability 0.71). MolNFT v1 #73792 on GenesisL1: 3D…

PDB: 3OCU
Type: protein
Length: 247 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipoprotein E
EC: 3.1.3.2
UniProt: P26093
Ligands: NMN, MG
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipoprotein E (EC 3.1.3.2)	protein	247	51% helix, 15% strand	P26093

Ligands and binding sites

NMN · Beta-nicotinamide ribose monophosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

3 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	473	0.71	0.81	62	MG, NMN
2	69	0.34	0.76	16	empty
3	78	0.31	0.73	15	empty

Compared structures

3OCU · Structure of Recombinant Haemophilus Influenzae e(P4) Acid Phosphatase mutant D66N… · the same entry in another collection · chain A against A, TM-score 1.00
P26093 · AlphaFold monomer V2.0 prediction for lipoprotein E (P26093) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P26093
Elsewhere: RCSB PDB 3OCU · PDBe 3OCU · UniProt P26093

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