Research workbench

Cleaved alpha-1-antitrypsin polymer

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

PDB: 1QMB
Type: protein
Length: 368 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-1-antitrypsin
UniProt: P01009
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-1-antitrypsin	protein	326	32% helix, 33% strand	P01009
B	Alpha-1-antitrypsin	protein	42	0% helix, 43% strand	P01009

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	171	0.72	0.89	20	empty

Interfaces

1 interface between chains.

A–B · 2330 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

1QMB · Cleaved alpha-1-antitrypsin polymer · 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 0.92

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 1QMB · PDBe 1QMB · UniProt P01009

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