MolNFT v1 · #174960 · protein

Blasnase-T13A with L-asp

7CBU · L-asparaginase: “Blasnase-T13A with L-asp”. X-ray diffraction, 2 ligands (ASP, MG), 5 pockets (best druggability 0.69). MolNFT v1 #174960 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7CBU
Type: protein
Length: 639 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-asparaginase
UniProt: A0A1Q8GMZ7
Ligands: ASP, MG
Pockets: 5 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-asparaginase	protein	318	30% helix, 24% strand	A0A1Q8GMZ7
B	L-asparaginase	protein	321	30% helix, 24% strand	A0A1Q8GMZ7

Ligands and binding sites

ASP · Aspartic acid · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 7 copies · chains A, B
FMT · Formic acid · additive · 4 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.69	0.92	29	empty
2	65	0.60	0.90	20	MG
3	75	0.55	0.87	30	ASP
4	172	0.53	0.79	32	empty
5	185	0.53	0.78	31	empty

Interfaces

1 interface between chains.

A–B · 3063 Å² buried · 53 hydrogen bonds · protein-protein

Compared structures

7CBU · Blasnase-T13A with L-Asp · 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 A0A1Q8GMZ7
Elsewhere: RCSB PDB 7CBU · PDBe 7CBU · UniProt A0A1Q8GMZ7

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