Research workbench

Crystal structure of mtbmgl K74A (closed cap conformation)

Analyse Crystal structure of mtbmgl K74A (closed cap conformation) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7OZM
Type: protein
Length: 278 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Monoacylglycerol lipase
EC: 3.1.1.23
UniProt: O07427
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Monoacylglycerol lipase (EC 3.1.1.23)	protein	278	42% helix, 21% strand	O07427

Ligands and binding sites

IPA · Isopropyl alcohol · 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	194	0.76	0.91	38	IPA
2	53	0.23	0.72	15	empty

Compared structures

7OZM · Crystal Structure of mtbMGL K74A (Closed Cap Conformation) · the same entry in another collection · chain A against A, TM-score 1.00
O07427 · AlphaFold monomer V2.0 prediction for monoacylglycerol lipase (O07427) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O07427
Elsewhere: RCSB PDB 7OZM · PDBe 7OZM · UniProt O07427

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