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Cold-adaption of enzymes: structural comparison between salmon and bovine trypsins

Analyse Cold-adaption of enzymes: structural comparison between salmon and bovine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2TBS
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trypsin
EC: 3.4.21.4
UniProt: P35031
Ligands: BEN, CA
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trypsin (EC 3.4.21.4)	protein	222	9% helix, 36% strand	P35031

Ligands and binding sites

BEN · Benzamidine · ligand · chains A
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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.32	0.77	16	empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

2TBS · Cold-adaption of enzymes: structural comparison between salmon and bovine trypsins · the same entry in another collection · chain A against A, TM-score 1.00
P35031 · AlphaFold monomer V2.0 prediction for trypsin-1 (P35031) · 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 P35031
Elsewhere: RCSB PDB 2TBS · PDBe 2TBS · UniProt P35031

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