MolNFT v1 · #116085 · protein

Directed evolutionary changes in kemp eliminase KE07 - crystal 6 ROUND5

5D2X · De novo desinged kemp eliminase KE07: “Directed evolutionary changes in kemp eliminase KE07 - crystal 6 ROUND5”. X-ray diffraction, 2 pockets (best druggability 0.64). MolNFT v1 #116085 on GenesisL1: 3D structure, binding sites and…

PDB: 5D2X
Type: protein
Length: 250 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: De novo desinged kemp eliminase KE07
Pockets: 2 · best druggability 0.64

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	De novo desinged kemp eliminase KE07	protein	250	40% helix, 25% strand	—

Ligands and binding sites

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

2 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	340	0.64	0.79	35	MPD
2	52	0.44	0.84	15	empty

Compared structures

5D2X · Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 6 Round5 · 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 5D2X · PDBe 5D2X

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