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Crystal structure of mouse angiotensinogen in the reduced form

Analyse Crystal structure of mouse angiotensinogen in the reduced form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WXY
Type: protein
Length: 419 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Angiotensinogen
UniProt: P11859
Ligands: NA
Pockets: 4 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Angiotensinogen	protein	419	30% helix, 32% strand	P11859

Ligands and binding sites

NA · Sodium ion · metal · 4 copies · chains C
EDO · 1,2-ethanediol · additive · 5 copies · chains C

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

Pockets

4 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	116	0.47	0.79	26	empty
2	55	0.31	0.76	14	empty
3	62	0.30	0.75	14	EDO, NA
4	66	0.29	0.73	15	empty

Compared structures

2WXY · Crystal structure of mouse angiotensinogen in the reduced form · the same entry in another collection · chain C against C, TM-score 1.00
P11859 · AlphaFold monomer V2.0 prediction for angiotensinogen (P11859) · a predicted model of the same protein · chain C against A, TM-score 0.98

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 P11859
Elsewhere: RCSB PDB 2WXY · PDBe 2WXY · UniProt P11859

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