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Structure of native pancreatic elastase from north atlantic salmon at 1.61 ångströms resolution

Analyse Structure of native pancreatic elastase from north atlantic salmon at 1.61… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ELT
Type: protein
Length: 236 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elastase
EC: 3.4.21.36
UniProt: Q7SIG3
Ligands: CA
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elastase (EC 3.4.21.36)	protein	236	11% helix, 36% strand	Q7SIG3

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

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	60	0.53	0.87	18	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1ELT · Structure of native pancreatic elastase from north atlantic salmon at 1.61 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
Q7SIG3 · AlphaFold monomer V2.0 prediction for elastase-1 (Q7SIG3) · a predicted model of the same protein · 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 Q7SIG3
Elsewhere: RCSB PDB 1ELT · PDBe 1ELT · UniProt Q7SIG3

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