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OMPTDELTAL8 (loop L8 deletion mutant of ompt), an outer membrane protein of vibrio cholerae

Analyse OMPTDELTAL8 (loop L8 deletion mutant of ompt), an outer membrane protein of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EHE
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ompt protein
UniProt: A0A0H3AME7
Ligands: MG
Pockets: 3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 71% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ompt protein	protein	302	2% helix, 71% strand	A0A0H3AME7

Ligands and binding sites

MG · Magnesium ion · metal · chains A
C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 8 copies · chains A
ACT · Acetate ion · additive · 2 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	228	0.43	0.72	37	MG
2	108	0.37	0.74	20	empty
3	76	0.29	0.73	18	empty

Compared structures

6EHE · OmpTdeltaL8 (loop L8 deletion mutant of OmpT), an outer membrane protein of Vibrio… · the same entry in another collection · 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 A0A0H3AME7
Elsewhere: RCSB PDB 6EHE · PDBe 6EHE · UniProt A0A0H3AME7

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