MolNFT v1 · #47753 · protein

The crystal structure of rhodesain, the major cysteine protease of T. brucei rhodesiense, bound to inhibitor K777

2P7U: “The crystal structure of rhodesain, the major cysteine protease of T. brucei rhodesiense, bound to inhibitor…”. X-ray diffraction, 1 ligand (D1R), 1 pocket (best druggability 0.30). MolNFT v1 #47753 on GenesisL1: 3D structure…

PDB: 2P7U
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine protease
UniProt: Q95PM0
Ligands: D1R
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cysteine protease	protein	215	28% helix, 23% strand	Q95PM0

Ligands and binding sites

D1R · Nalpha-[(4-methylpiperazin-1-yl)carbonyl]-N-{(1S)-3-phenyl-1-[2-(phenylsulfonyl)ethyl]propyl}-L-phenylalaninamide · ligand · 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	67	0.30	0.74	17	empty

Modifications

Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

2P7U · The crystal structure of rhodesain, the major cysteine protease of T. brucei rhodesiense… · 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 Q95PM0
Elsewhere: RCSB PDB 2P7U · PDBe 2P7U · UniProt Q95PM0

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