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Crystal structure of EST25 - a bacterial homolog of hormone-sensitive lipase from a metagenomic library

Analyse Crystal structure of EST25 - a bacterial homolog of hormone-sensitive lipase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J7A
Type: protein
Length: 1,420 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
UniProt: Q4TZQ3
Pockets: 13 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Esterase	protein	355	41% helix, 16% strand	Q4TZQ3

Pockets

13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.78	0.97	24	empty
2	221	0.74	0.89	36	empty
3	674	0.73	0.80	49	empty
4	751	0.72	0.78	52	empty
5	247	0.70	0.85	43	empty

Interfaces

3 interfaces between chains.

A–D · 1158 Å² buried · 17 hydrogen bonds · protein-protein
B–C · 1056 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 337 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4J7A · Crystal Structure of Est25 - a Bacterial Homolog of Hormone-Sensitive Lipase from a… · 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 Q4TZQ3
Elsewhere: RCSB PDB 4J7A · PDBe 4J7A · UniProt Q4TZQ3

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