MolNFT v1 · #174935 · protein

Crystal structures of of blasnase

7CB4 · L-asparaginase: “Crystal structures of of blasnase”. X-ray diffraction, 1 ligand (MG), 5 pockets (best druggability 0.71). MolNFT v1 #174935 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7CB4
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: MG
Pockets: 5 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	L-asparaginase	protein	321	31% helix, 24% strand	A0A1Q8GMZ7
A	L-asparaginase	protein	318	31% helix, 24% strand	A0A1Q8GMZ7

Ligands and binding sites

MG · Magnesium ion · metal · 6 copies · chains B, A
FMT · Formic acid · additive · 5 copies · chains B, A
GOL · Glycerol · additive · 2 copies · chains B, A

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

Pockets

5 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	148	0.71	0.91	44	MG
2	157	0.52	0.79	26	empty
3	184	0.52	0.78	30	empty
4	79	0.42	0.80	30	FMT, GOL
5	51	0.26	0.73	14	empty

Interfaces

1 interface between chains.

B–A · 3010 Å² buried · 56 hydrogen bonds · protein-protein

Compared structures

7CB4 · Crystal structures of of BlAsnase · the same entry in another collection · chain B against B, 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 7CB4 · PDBe 7CB4 · UniProt A0A1Q8GMZ7

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