MolNFT v1 · #148859 · protein

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

6FJ2: “Structure of thermolysin solved from sad data collected at the peak of the zn absorption edge on ID30B”. X-ray diffraction, 3 ligands (TMO, CA, ZN), 1 pocket (best druggability 0.27). MolNFT v1 #148859 on GenesisL1: 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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