MolNFT v1 · #1130 · protein

Cleaved antichymotrypsin A349R

1AS4: “Cleaved antichymotrypsin A349R”. X-ray diffraction, 2 pockets (best druggability 0.38). MolNFT v1 #1130 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1AS4
Type: protein
Length: 369 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antichymotrypsin
UniProt: P01011
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Antichymotrypsin	protein	336	34% helix, 38% strand	P01011
B	Antichymotrypsin	protein	33	0% helix, 48% strand	P01011

Ligands and binding sites

ACT · Acetate ion · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.38	0.75	21	empty
2	68	0.38	0.78	18	empty

Interfaces

1 interface between chains.

A–B · 2470 Å² buried · 45 hydrogen bonds · protein-protein

Compared structures

1AS4 · Cleaved antichymotrypsin A349R · 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 0.94

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 1AS4 · PDBe 1AS4 · UniProt P01011

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