MolNFT v1 · #147572 · protein

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

6EHE · Ompt protein: “OMPTDELTAL8 (loop L8 deletion mutant of ompt), an outer membrane protein of vibrio cholerae”. X-ray diffraction, 1 ligand (MG), 3 pockets (best druggability 0.43). MolNFT v1 #147572 on GenesisL1: 3D structure, binding…

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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