MolNFT v1 · #71238 · protein

Crystal structure of the cysteine protease inhibitor, EHICP2, from entamoeba histolytica

3M86 · Amoebiasin-2: “Crystal structure of the cysteine protease inhibitor, EHICP2, from entamoeba histolytica”. X-ray diffraction, 2 ligands (CL, SO4), 2 pockets (best druggability 0.46). MolNFT v1 #71238 on GenesisL1: 3D structure…

PDB: 3M86
Type: protein
Length: 215 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amoebiasin-2
UniProt: C4M2H5
Ligands: CL, SO4
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amoebiasin-2	protein	111	5% helix, 53% strand	C4M2H5
B	Amoebiasin-2	protein	104	6% helix, 54% strand	C4M2H5

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains B
1PE · Pentaethylene glycol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	174	0.46	0.75	24	empty
2	111	0.36	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 261 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3M86 · Crystal structure of the cysteine protease inhibitor, EhICP2, from Entamoeba histolytica · 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 C4M2H5
Elsewhere: RCSB PDB 3M86 · PDBe 3M86 · UniProt C4M2H5

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