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Cryo-EM structure of E. COLI ompf

Analyse Cryo-EM structure of E. COLI ompf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WTZ
Type: protein
Length: 1,020 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer membrane porin F
UniProt: P02931
Pockets: 10 · best druggability 0.71

Structure

electron microscopy · 1 distinct chain · 3% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Outer membrane porin F	protein	340	3% helix, 55% strand	P02931

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1034	0.71	0.75	74	empty
2	1023	0.71	0.75	66	empty
3	1036	0.71	0.75	69	empty
4	241	0.47	0.74	33	empty
5	230	0.47	0.74	38	empty

Interfaces

3 interfaces between chains.

A–C · 1493 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 1491 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1485 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6WTZ · Cryo-EM structure of E. Coli OmpF · 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 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 P02931
Elsewhere: RCSB PDB 6WTZ · PDBe 6WTZ · UniProt P02931

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