MolNFT v1 · #154630 · protein

Lipase (closed form)

6KHK · Hydrolase, ALPHA/BETA domain protein: “Lipase (closed form)”. X-ray diffraction, 5 pockets (best druggability 0.83). MolNFT v1 #154630 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6KHK
Type: protein
Length: 619 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrolase, ALPHA/BETA domain protein
UniProt: E6DAE5
Pockets: 5 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydrolase, ALPHA/BETA domain protein	protein	310	44% helix, 17% strand	E6DAE5
B	Hydrolase, ALPHA/BETA domain protein	protein	309	43% helix, 17% strand	E6DAE5

Ligands and binding sites

GOL · Glycerol · additive · 10 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	446	0.83	0.90	59	empty
2	86	0.76	0.97	22	GOL
3	86	0.76	0.97	22	GOL
4	109	0.53	0.82	22	GOL
5	122	0.48	0.79	23	empty

Interfaces

1 interface between chains.

A–B · 1171 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6KHK · Lipase (Closed form) · 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 E6DAE5
Elsewhere: RCSB PDB 6KHK · PDBe 6KHK · UniProt E6DAE5

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