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Directed evolutionary changes in kemp eliminase KE07 - crystal 28 round 5

Analyse Directed evolutionary changes in kemp eliminase KE07 - crystal 28 round 5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DNJ
Type: protein
Length: 250 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kemp eliminase KE07
Ligands: H5J
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kemp eliminase KE07	protein	250	40% helix, 25% strand	—

Ligands and binding sites

H5J · 5-nitro-1,2-benzoxazole · ligand · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	384	0.67	0.80	48	MPD, H5J

Compared structures

6DNJ · Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 28 round 5 · 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
Elsewhere: RCSB PDB 6DNJ · PDBe 6DNJ

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