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Structure of human nnmt in complex with macrocyclic peptide X

Analyse Structure of human nnmt in complex with macrocyclic peptide X in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EGU
Type: protein
Length: 259 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nicotinamide N-methyltransferase; Macrocyclic peptide X
EC: 2.1.1.1
UniProt: P40261
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nicotinamide N-methyltransferase (EC 2.1.1.1)	protein	248	37% helix, 29% strand	P40261
B	Macrocyclic peptide X	protein	11	0% helix, 0% strand	—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.27	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 1050 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

7EGU · Structure of human NNMT in complex with macrocyclic peptide X · the same entry in another collection · chain A against A, TM-score 1.00
P40261 · AlphaFold monomer V2.0 prediction for nicotinamide N-methyltransferase (P40261) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P40261
Elsewhere: RCSB PDB 7EGU · PDBe 7EGU · UniProt P40261

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