Research workbench

Human bleomycin hydrolase.

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

PDB: 1CB5
Type: protein
Length: 1,359 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bleomycin hydrolase
EC: 3.4.22.-
UniProt: Q13867
Pockets: 20 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Bleomycin hydrolase (EC 3.4.22.-)	protein	453	45% helix, 17% strand	Q13867

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	784	0.68	0.75	61	empty
2	667	0.67	0.76	46	empty
3	602	0.66	0.76	47	empty
4	105	0.56	0.84	22	empty
5	99	0.56	0.85	22	empty

Interfaces

3 interfaces between chains.

B–C · 583 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 554 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 540 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1CB5 · Human bleomycin hydrolase. · 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 1CB5 · PDBe 1CB5 · UniProt Q13867

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