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Crystal structure of an alpha-1-antitrypsin trimer

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

PDB: 3T1P
Type: protein
Length: 371 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-1-antitrypsin
UniProt: P01009
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-1-antitrypsin	protein	371	28% helix, 34% strand	P01009

Pockets

2 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	894	0.78	0.80	61	empty
2	73	0.41	0.79	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3T1P · Crystal structure of an alpha-1-antitrypsin trimer · 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 0.82

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 3T1P · PDBe 3T1P · UniProt P01009

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