Research workbench

Blasnase-T13A with L-asn

Analyse Blasnase-T13A with L-asn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C8X
Type: protein
Length: 639 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Asparaginase
UniProt: A0A2V2HLK7
Ligands: ASN, MG
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Asparaginase	protein	319	31% helix, 24% strand	A0A2V2HLK7
B	Asparaginase	protein	320	30% helix, 24% strand	A0A2V2HLK7

Ligands and binding sites

ASN · Asparagine · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 7 copies · chains A, B
FMT · Formic acid · additive · 6 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	161	0.75	0.92	46	MG
2	66	0.54	0.87	27	ASN, FMT
3	143	0.52	0.80	25	empty
4	133	0.49	0.79	26	empty

Interfaces

1 interface between chains.

A–B · 3057 Å² buried · 51 hydrogen bonds · protein-protein

Compared structures

7C8X · Blasnase-T13A with L-asn · 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 A0A2V2HLK7
Elsewhere: RCSB PDB 7C8X · PDBe 7C8X · UniProt A0A2V2HLK7

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