Research workbench

SAV1875-cysteinesulfonic acid

Analyse SAV1875-cysteinesulfonic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Y1R
Type: protein
Length: 340 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein SAV1875
UniProt: P0A0K0
Pockets: 2 · best druggability 0.32

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein SAV1875	protein	171	36% helix, 23% strand	P0A0K0
B	Uncharacterized protein SAV1875	protein	169	38% helix, 22% strand	P0A0K0

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	70	0.32	0.75	17	empty
2	63	0.31	0.76	20	empty

Interfaces

1 interface between chains.

A–B · 883 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

4Y1R · SAV1875-cysteinesulfonic acid · the same entry in another collection · chain A against A, TM-score 1.00
P0A0K0 · AlphaFold monomer V2.0 prediction for uncharacterized protein SAV1875 (P0A0K0) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P0A0K0
Elsewhere: RCSB PDB 4Y1R · PDBe 4Y1R · UniProt P0A0K0

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