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Crystal structure of ALPHA1-antichymotrypsin variant newbg-0: a new binding globulin variant that is devoid of any cortisol-binding capabilities

Analyse Crystal structure of ALPHA1-antichymotrypsin variant newbg-0: a new binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HGD
Type: protein
Length: 373 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-1-antichymotrypsin
UniProt: P01011
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-1-antichymotrypsin	protein	336	32% helix, 37% strand	P01011
B	Alpha-1-antichymotrypsin	protein	37	0% helix, 46% strand	P01011

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	74	0.35	0.76	20	empty

Interfaces

1 interface between chains.

A–B · 2486 Å² buried · 33 hydrogen bonds · protein-protein

Compared structures

6HGD · Crystal structure of Alpha1-antichymotrypsin variant NewBG-0: a new binding globulin… · the same entry in another collection · chain A against A, TM-score 1.00
P01011 · AlphaFold monomer V2.0 prediction for alpha-1-antichymotrypsin (P01011) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P01011
Elsewhere: RCSB PDB 6HGD · PDBe 6HGD · UniProt P01011

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