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Radiation damage study of thermolysin - 100K structure D (7.2 MGy)

Analyse Radiation damage study of thermolysin - 100K structure D (7.2 MGy) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P7S
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.2
Source: Bacillus thermoproteolyticus
Molecule: Thermolysin
EC: 3.4.24.27
UniProt: P00800
Ligands: CA, ZN
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · resolution 2.2 · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Thermolysin (EC 3.4.24.27)	protein	316	41% helix, 18% strand	P00800

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains E
ZN · Zinc ion · metal · chains E

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	62	0.42	0.81	16	empty
2	60	0.36	0.78	14	empty

Compared structures

3P7S · Radiation damage study of thermolysin - 100K structure D (7.2 mgy) · the same entry in another collection · chain E against E, TM-score 1.00
P00800 · AlphaFold monomer V2.0 prediction for thermolysin (P00800) · a predicted model of the same protein · chain E 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 3P7S · PDBe 3P7S · UniProt P00800

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