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Structure of the apo form of ycni

Analyse Structure of the apo form of ycni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ME6
Type: protein
Length: 257 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein ycni
UniProt: P94431
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein ycni	protein	129	0% helix, 57% strand	P94431
B	Uncharacterized protein ycni	protein	128	0% helix, 57% strand	P94431

Ligands and binding sites

MLI · Malonate ion · additive · 2 copies · chains A, 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	113	0.38	0.75	24	empty
2	74	0.31	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 495 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7ME6 · Structure of the apo form of YcnI · the same entry in another collection · chain A against A, TM-score 1.00
P94431 · AlphaFold monomer V2.0 prediction for uncharacterized protein ycni (P94431) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P94431
Elsewhere: RCSB PDB 7ME6 · PDBe 7ME6 · UniProt P94431

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