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Crystal structure of alpha-1-antitrypsin, crystal form a

Analyse Crystal structure of alpha-1-antitrypsin, crystal form a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QUG
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 0.60

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-1-antitrypsin	protein	369	30% helix, 31% strand	P01009

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	68	0.60	0.90	20	empty
2	50	0.36	0.80	15	empty
3	86	0.32	0.73	17	empty
4	63	0.32	0.75	13	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

2QUG · Crystal structure of alpha-1-antitrypsin, crystal form A · 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 0.99

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 2QUG · PDBe 2QUG · UniProt P01009

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