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Crystal structure of pepw from lactobacillus rhamnosis HN001 (DR20) determined as the selenomet derivative

Analyse Crystal structure of pepw from lactobacillus rhamnosis HN001 (DR20) determined… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4K7C
Type: protein
Length: 446 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminopeptidase C
EC: 3.4.22.-
UniProt: B5QNU9
Pockets: 5 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminopeptidase C (EC 3.4.22.-)	protein	446	46% helix, 18% strand	B5QNU9

Ligands and binding sites

GOL · Glycerol · additive · 8 copies · chains A

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

Pockets

5 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	159	0.66	0.86	24	empty
2	106	0.48	0.80	19	GOL
3	154	0.42	0.74	15	empty
4	62	0.34	0.77	21	empty
5	57	0.33	0.77	17	empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

4K7C · Crystal structure of pepw from lactobacillus rhamnosis hn001 (dr20) determined as the… · 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 B5QNU9
Elsewhere: RCSB PDB 4K7C · PDBe 4K7C · UniProt B5QNU9

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