MolNFT v1 · #70219 · protein

Structure of arabidopsis ATSERPIN1. native stressed conformation

3LE2 · Serpin-zx: “Structure of arabidopsis ATSERPIN1. native stressed conformation”. X-ray diffraction, 1 ligand (SO4), 5 pockets (best druggability 0.49). MolNFT v1 #70219 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3LE2
Type: protein
Length: 393 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serpin-zx
UniProt: Q9S7T8
Ligands: SO4
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serpin-zx	protein	393	32% helix, 30% strand	Q9S7T8

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
ACT · Acetate ion · additive · 2 copies · chains A
GOL · Glycerol · additive · chains 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	80	0.49	0.83	24	empty
2	71	0.47	0.83	17	empty
3	72	0.47	0.82	22	GOL
4	60	0.44	0.83	17	empty
5	63	0.32	0.76	13	empty

Compared structures

3LE2 · Structure of Arabidopsis AtSerpin1. Native Stressed Conformation · the same entry in another collection · chain A against A, TM-score 1.00
Q9S7T8 · AlphaFold monomer V2.0 prediction for serpin-zx (Q9S7T8) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9S7T8
Elsewhere: RCSB PDB 3LE2 · PDBe 3LE2 · UniProt Q9S7T8

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