Research workbench

Cleaved antitrypsin with P10 pro, and P9-P6 asp

Analyse Cleaved antitrypsin with P10 pro, and P9-P6 asp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NDD
Type: protein
Length: 370 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 0.50

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-1-antitrypsin	protein	335	33% helix, 36% strand	P01009
B	Alpha-1-antitrypsin	protein	35	0% helix, 49% strand	P01009

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	105	0.50	0.81	21	empty

Interfaces

1 interface between chains.

A–B · 2437 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

3NDD · Cleaved antitrypsin with P10 Pro, and P9-P6 Asp · 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 0.91

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 3NDD · PDBe 3NDD · UniProt P01009

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