MolNFT v1 · #3354 · protein

Crystal structures of recombinant rat cathepsin B and a cathepsin B- inhibitor complex: implications for structure-based inhibitor design

1CPJ: “Crystal structures of recombinant rat cathepsin B and a cathepsin B- inhibitor complex: implications for…”. X-ray diffraction, 2 pockets (best druggability 0.77). MolNFT v1 #3354 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1CPJ
Type: protein
Length: 506 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cathepsin B
EC: 3.4.22.1
UniProt: P00787
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cathepsin B (EC 3.4.22.1)	protein	253	24% helix, 24% strand	P00787

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1085	0.77	0.79	96	empty
2	60	0.32	0.77	22	empty

Interfaces

1 interface between chains.

A–B · 832 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

1CPJ · Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex… · the same entry in another collection · chain A against A, TM-score 1.00
P00787 · AlphaFold monomer V2.0 prediction for cathepsin B (P00787) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P00787
Elsewhere: RCSB PDB 1CPJ · PDBe 1CPJ · UniProt P00787

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