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Crystal structure of cold-active estarase from psychrobacter cryohalolentis K5T

Analyse Crystal structure of cold-active estarase from psychrobacter cryohalolentis K5T in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NS4
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA/BETA hydrolase fold protein
EC: 3.1.1.6
UniProt: Q1QEU6
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA/BETA hydrolase fold protein (EC 3.1.1.6)	protein	271	42% helix, 18% strand	Q1QEU6

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	495	0.83	0.89	60	empty

Compared structures

4NS4 · Crystal structure of cold-active estarase from Psychrobacter cryohalolentis K5T · 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 Q1QEU6
Elsewhere: RCSB PDB 4NS4 · PDBe 4NS4 · UniProt Q1QEU6

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