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Use of the neutron diffraction H/D exchange technique to determine the conformational dynamics of trypsin

Analyse Use of the neutron diffraction H/D exchange technique to determine the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NTP
Type: protein
Length: 223 residues
Chains: 1
Method: neutron diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-trypsin
EC: 3.4.21.4
UniProt: P00760
Ligands: ISP
Pockets: 2 · best druggability 0.42

Structure

neutron diffraction · 1 distinct chain · 10% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-trypsin (EC 3.4.21.4)	protein	223	10% helix, 36% strand	P00760

Ligands and binding sites

ISP · Phosphorylisopropane · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.42	0.81	20	empty
2	58	0.31	0.76	18	ISP

Modifications

Observed in the structure: 6 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

1NTP · Use of the neutron diffraction H/D exchange technique to determine the conformational… · 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 P00760
Elsewhere: RCSB PDB 1NTP · PDBe 1NTP · UniProt P00760

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