MolNFT v1 · #106692 · protein

Slow-and fast-binding inhibitors of thermolysin display different modes of binding. crystallographic analysis of extended phosphonamidate transition-state analogues

4TMN: “Slow-and fast-binding inhibitors of thermolysin display different modes of binding. crystallographic analysis…”. X-ray diffraction, 3 ligands (0PK, CA, ZN), 1 pocket (best druggability 0.51). MolNFT v1 #106692 on GenesisL1: 3D…

PDB: 4TMN
Type: protein
Length: 316 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: 0PK, CA, ZN
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Thermolysin (EC 3.4.24.27)	protein	316	41% helix, 17% strand	P00800

Ligands and binding sites

0PK · N-[(S)-[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl]-L-leucyl-L-alanine · ligand · chains E
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

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	128	0.51	0.81	23	0PK

Compared structures

4TMN · Slow-and fast-binding inhibitors of thermolysin display different modes of binding.… · 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 4TMN · PDBe 4TMN · UniProt P00800

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