MolNFT v1 · #119326 · protein

Structure of thermolysin prepared by the 'soak-and-freeze' method under 40 bar of krypton pressure

5FSS: “Structure of thermolysin prepared by the 'soak-and-freeze' method under 40 bar of krypton pressure”. X-ray diffraction, 3 ligands (CA, ZN, KR), 2 pockets (best druggability 0.30). MolNFT v1 #119326 on GenesisL1: 3D structure…

PDB: 5FSS
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, KR
Pockets: 2 · best druggability 0.30

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thermolysin (EC 3.4.24.27)	protein	318	42% helix, 18% strand	P00800

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A
ZN · Zinc ion · metal · 2 copies · chains A
KR · Krypton · ion · 2 copies · chains A
GOL · Glycerol · additive · 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	55	0.30	0.75	16	empty
2	55	0.30	0.76	17	ZN

Compared structures

5FSS · Structure of thermolysin prepared by the 'soak-and-freeze' method under 40 bar of krypton… · 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 5FSS · PDBe 5FSS · UniProt P00800

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