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Studies on crystal structures active center geometry and depurine mechanism of two ribosome-inactivating proteins

Analyse Studies on crystal structures active center geometry and depurine mechanism of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MRG
Type: protein
Length: 246 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-momorcharin
UniProt: P16094
Ligands: ADN
Pockets: 2 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-momorcharin	protein	246	42% helix, 24% strand	P16094

Ligands and binding sites

ADN · Adenosine · ligand · chains A

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	133	0.45	0.77	22	ADN
2	58	0.32	0.76	12	empty

Compared structures

1MRG · Studies on crystal structures active center geometry and depurine mechanism of two… · the same entry in another collection · chain A against A, TM-score 1.00
P16094 · AlphaFold monomer V2.0 prediction for ribosome-inactivating protein momordin I (P16094) · 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 P16094
Elsewhere: RCSB PDB 1MRG · PDBe 1MRG · UniProt P16094

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