MolNFT v1 · #134620 · protein

Conformational sampling differences across the arrhenius plot biphasic break point at ambient temperature in the enzyme thermolysin

5T9Q: “Conformational sampling differences across the arrhenius plot biphasic break point at ambient temperature in…”. X-ray diffraction, 3 ligands (CA, ZN, PO4), 1 pocket (best druggability 0.31). MolNFT v1 #134620 on GenesisL1: 3D…

PDB: 5T9Q
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thermolysin
EC: 3.4.24.27
UniProt: P00800
Ligands: CA, ZN, PO4
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thermolysin (EC 3.4.24.27)	protein	318	41% helix, 18% strand	P00800

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A
ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · 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	64	0.31	0.75	16	PO4

Compared structures

5T9Q · Conformational Sampling Differences across the Arrhenius Plot Biphasic Break Point at… · 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 P00800
Elsewhere: RCSB PDB 5T9Q · PDBe 5T9Q · UniProt P00800

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.