MolNFT v1 · #101850 · protein

Crystal structure of uncleaved guinea pig L-asparaginase type III

4O47 · Uncharacterized protein: “Crystal structure of uncleaved guinea pig L-asparaginase type III”. X-ray diffraction, 1 ligand (NA), 6 pockets (best druggability 0.54). MolNFT v1 #101850 on GenesisL1: 3D structure, binding sites and…

PDB: 4O47
Type: protein
Length: 585 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
EC: 3.5.1.1
UniProt: H0VQC8
Ligands: NA
Pockets: 6 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein (EC 3.5.1.1)	protein	295	35% helix, 26% strand	H0VQC8
B	Uncharacterized protein (EC 3.5.1.1)	protein	290	35% helix, 27% strand	H0VQC8

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.54	0.87	20	empty
2	111	0.51	0.81	17	empty
3	189	0.50	0.77	33	empty
4	113	0.47	0.80	27	empty
5	92	0.46	0.80	14	empty

Interfaces

1 interface between chains.

A–B · 1750 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

4O47 · Crystal structure of uncleaved guinea pig L-asparaginase type III · 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 H0VQC8
Elsewhere: RCSB PDB 4O47 · PDBe 4O47 · UniProt H0VQC8

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