Research workbench

OMPF PORIN

Analyse OMPF PORIN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K19
Type: protein
Length: 4,080 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer membrane protein F
UniProt: P02931
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Outer membrane protein F	protein	340	6% helix, 59% strand	P02931

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1015	0.79	0.81	104	empty
2	798	0.78	0.82	84	empty
3	806	0.77	0.81	83	empty
4	1190	0.76	0.79	124	empty
5	941	0.70	0.75	64	empty

Interfaces

30 interfaces between chains.

B–C · 1531 Å² buried · 17 hydrogen bonds · protein-protein
D–F · 1527 Å² buried · 17 hydrogen bonds · protein-protein
J–K · 1524 Å² buried · 17 hydrogen bonds · protein-protein
H–I · 1522 Å² buried · 16 hydrogen bonds · protein-protein
G–I · 1521 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

3K19 · OmpF porin · the same entry in another collection · chain L against L, 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 3K19 · PDBe 3K19 · UniProt P02931

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