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Blasnase-T13A with D-asn

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

PDB: 7CBW
Type: protein
Length: 642 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 0.65

Structure

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

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

Ligands and binding sites

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

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.65	0.92	29	MG
2	57	0.56	0.89	20	MG
3	173	0.52	0.79	27	empty
4	173	0.52	0.78	32	empty
5	51	0.25	0.73	15	empty

Interfaces

1 interface between chains.

A–B · 3015 Å² buried · 51 hydrogen bonds · protein-protein

Compared structures

7CBW · Blasnase-T13A with D-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 A0A1Q8GMZ7
Elsewhere: RCSB PDB 7CBW · PDBe 7CBW · UniProt A0A1Q8GMZ7

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