Research workbench

Ompf porin deletion (mutant delta 109-114)

Analyse Ompf porin deletion (mutant delta 109-114) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GFN
Type: protein
Length: 327 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Matrix porin outer membrane protein F
UniProt: P02931
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 62% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Matrix porin outer membrane protein F	protein	327	5% helix, 62% strand	P02931

Ligands and binding sites

C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 12 copies · chains A

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

Pockets

4 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	469	0.65	0.78	53	empty
2	202	0.47	0.75	42	empty
3	134	0.42	0.75	20	empty
4	83	0.33	0.74	14	empty

Compared structures

1GFN · Ompf porin deletion (mutant delta 109-114) · the same entry in another collection · chain A against A, TM-score 1.00
P02931 · AlphaFold monomer V2.0 prediction for outer membrane porin F (P02931) · 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 P02931
Elsewhere: RCSB PDB 1GFN · PDBe 1GFN · UniProt P02931

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