Research workbench

Human bleomycin hydrolase, C73S/DELE455 mutant

Analyse Human bleomycin hydrolase, C73S/DELE455 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CB5
Type: protein
Length: 906 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (bleomycin hydrolase)
EC: 3.4.22.-
UniProt: Q13867
Pockets: 11 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein (bleomycin hydrolase) (EC 3.4.22.-)	protein	453	44% helix, 18% strand	Q13867

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	479	0.63	0.76	52	empty
2	157	0.58	0.82	27	empty
3	146	0.56	0.82	28	empty
4	92	0.43	0.79	16	empty
5	70	0.42	0.81	13	empty

Interfaces

1 interface between chains.

A–B · 287 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2CB5 · Human bleomycin hydrolase, C73S/DELE455 mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q13867 · AlphaFold monomer V2.0 prediction for bleomycin hydrolase (Q13867) · a predicted model of the same protein · 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 Q13867
Elsewhere: RCSB PDB 2CB5 · PDBe 2CB5 · UniProt Q13867

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.