MolNFT v1 · #121217 · protein

1.65 ångström resolution crystal structure of LMO0182 (residues 1-245) from listeria monocytogenes egd-E

5HOP · LMO0182 protein: “1.65 ångström resolution crystal structure of LMO0182 (residues 1-245) from listeria monocytogenes egd-E”. X-ray diffraction, 4 pockets (best druggability 0.73). MolNFT v1 #121217 on GenesisL1: 3D structure…

PDB: 5HOP
Type: protein
Length: 478 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LMO0182 protein
UniProt: Q8YAE8
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	LMO0182 protein	protein	239	62% helix, 7% strand	Q8YAE8

Ligands and binding sites

ACT · Acetate ion · additive · 2 copies · chains A, B

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	854	0.73	0.78	66	ACT
2	52	0.39	0.82	15	empty
3	90	0.38	0.76	19	empty
4	66	0.37	0.78	17	empty

Interfaces

1 interface between chains.

A–B · 197 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

5HOP · 1.65 Angstrom resolution crystal structure of lmo0182 (residues 1-245) from Listeria… · 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 Q8YAE8
Elsewhere: RCSB PDB 5HOP · PDBe 5HOP · UniProt Q8YAE8

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