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Structure of thermolysin solved from sad data collected at the peak of the zn absorption edge on ID30B

Analyse Structure of thermolysin solved from sad data collected at the peak of the zn… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FJ2
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: TMO, CA, ZN
Pockets: 1 · best druggability 0.27

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

TMO · trimethylamine oxide · ligand · 4 copies · chains A
CA · Calcium ion · metal · 4 copies · chains A
ZN · Zinc ion · metal · chains A
DMS · Dimethyl sulfoxide · additive · 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	57	0.27	0.74	20	empty

Compared structures

6FJ2 · Structure of Thermolysin solved from SAD data collected at the peak of the Zn absorption… · 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 6FJ2 · PDBe 6FJ2 · UniProt P00800

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