MolNFT v1 · #127953 · protein

Crystal structure of native alpha-1-antitrypsin with seven stabilising mutations

5NBV: “Crystal structure of native alpha-1-antitrypsin with seven stabilising mutations”. X-ray diffraction, 4 pockets (best druggability 0.54). MolNFT v1 #127953 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5NBV
Type: protein
Length: 369 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-1-antitrypsin
UniProt: P01009
Pockets: 4 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-1-antitrypsin	protein	369	29% helix, 30% strand	P01009

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.54	0.88	21	empty
2	52	0.44	0.83	14	GOL
3	59	0.31	0.76	16	empty
4	55	0.30	0.75	14	empty

Compared structures

5NBV · Crystal structure of native alpha-1-antitrypsin with seven stabilising mutations · the same entry in another collection · chain A against A, TM-score 1.00
P01009 · AlphaFold monomer V2.0 prediction for alpha-1-antitrypsin (P01009) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P01009
Elsewhere: RCSB PDB 5NBV · PDBe 5NBV · UniProt P01009

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