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Xray structure of domain-swapped cystatin E dimer

Analyse Xray structure of domain-swapped cystatin E dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FK0
Type: protein
Length: 224 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cystatin-M
UniProt: Q15828
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cystatin-M	protein	113	20% helix, 50% strand	Q15828
B	Cystatin-M	protein	111	21% helix, 50% strand	Q15828

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	57	0.30	0.75	11	empty

Interfaces

1 interface between chains.

A–B · 3512 Å² buried · 61 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

6FK0 · Xray structure of domain-swapped cystatin E dimer · the same entry in another collection · chain A against A, TM-score 1.00
Q15828 · AlphaFold monomer V2.0 prediction for cystatin-M (Q15828) · a predicted model of the same protein · chain A against A, TM-score 0.54

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 Q15828
Elsewhere: RCSB PDB 6FK0 · PDBe 6FK0 · UniProt Q15828

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