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Crystal structure of monomeric human cystatin C stabilized against aggregation

Analyse Crystal structure of monomeric human cystatin C stabilized against aggregation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GAX
Type: protein
Length: 214 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cystatin-C
UniProt: P01034
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cystatin-C	protein	107	20% helix, 51% strand	P01034
B	Cystatin-C	protein	107	22% helix, 50% strand	P01034

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.52	0.81	21	empty
2	71	0.46	0.83	18	empty
3	52	0.38	0.81	15	empty

Interfaces

1 interface between chains.

A–B · 992 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

3GAX · Crystal structure of monomeric human cystatin C stabilized against aggregation · the same entry in another collection · chain A against A, TM-score 1.00
P01034 · AlphaFold monomer V2.0 prediction for cystatin-C (P01034) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P01034
Elsewhere: RCSB PDB 3GAX · PDBe 3GAX · UniProt P01034

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