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Crystal structure of extracelular lipase from streptomyces rimosus at 1.7A resolution

Analyse Crystal structure of extracelular lipase from streptomyces rimosus at 1.7A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MAL
Type: protein
Length: 468 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase
EC: 3.1.1.3, 3.1.1.-, 3.1.2.2
UniProt: Q93MW7
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase (EC 3.1.1.3, 3.1.1.-, 3.1.2.2)	protein	234	49% helix, 12% strand	Q93MW7

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	781	0.75	0.80	71	empty
2	109	0.51	0.81	22	empty
3	105	0.39	0.76	24	empty

Interfaces

1 interface between chains.

A–B · 520 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

5MAL · Crystal structure of extracelular lipase from Streptomyces rimosus at 1.7A resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q93MW7 · AlphaFold monomer V2.0 prediction for lipase (Q93MW7) · 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 Q93MW7
Elsewhere: RCSB PDB 5MAL · PDBe 5MAL · UniProt Q93MW7

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