MolNFT v1 · #174862 · protein

Blasnase-T13A with D-asn

7C8Q · Asparaginase: “Blasnase-T13A with D-asn”. X-ray diffraction, 2 ligands (DSG, MG), 4 pockets (best druggability 0.72). MolNFT v1 #174862 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7C8Q
Type: protein
Length: 642 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Asparaginase
UniProt: A0A2V2HLK7
Ligands: DSG, MG
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Asparaginase	protein	321	31% helix, 24% strand	A0A2V2HLK7

Ligands and binding sites

DSG · D-asparagine · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 7 copies · chains A, B
FMT · Formic acid · additive · 5 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	146	0.72	0.91	43	MG
2	192	0.55	0.79	29	empty
3	187	0.54	0.79	30	empty
4	59	0.46	0.84	26	FMT, DSG

Interfaces

1 interface between chains.

A–B · 3081 Å² buried · 54 hydrogen bonds · protein-protein

Compared structures

7C8Q · Blasnase-T13A with D-asn · 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 A0A2V2HLK7
Elsewhere: RCSB PDB 7C8Q · PDBe 7C8Q · UniProt A0A2V2HLK7

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