Research workbench

E1M, A104W mutant of rh. blastica porin

Analyse E1M, A104W mutant of rh. blastica porin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PRN
Type: protein
Length: 289 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Porin
UniProt: P39767
Ligands: MG
Pockets: 3 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Porin	protein	289	4% helix, 54% strand	P39767

Ligands and binding sites

MG · Magnesium ion · metal · chains A
C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	91	0.33	0.74	24	empty
2	74	0.32	0.75	16	empty
3	76	0.28	0.72	18	empty

Compared structures

3PRN · E1M, A104W mutant of rh. blastica porin · the same entry in another collection · chain A against A, TM-score 1.00
P39767 · AlphaFold monomer V2.0 prediction for porin (P39767) · a predicted model of the same protein · 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 P39767
Elsewhere: RCSB PDB 3PRN · PDBe 3PRN · UniProt P39767

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