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X-ray diffraction analysis of the csstefin-1

Analyse X-ray diffraction analysis of the csstefin-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZC1
Type: protein
Length: 596 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cystatin-1
UniProt: A6YID9
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 21% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cystatin-1	protein	101	21% helix, 40% strand	A6YID9
C	Cystatin-1	protein	100	19% helix, 37% strand	A6YID9
D, E, F	Cystatin-1	protein	98	22% helix, 36% strand	A6YID9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	749	0.75	0.80	79	empty
2	156	0.66	0.87	23	empty
3	95	0.33	0.73	21	empty
4	54	0.28	0.74	17	empty

Interfaces

11 interfaces between chains.

A–E · 355 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 340 Å² buried · 3 hydrogen bonds · protein-protein
A–F · 337 Å² buried · 2 hydrogen bonds · protein-protein
B–E · 334 Å² buried · 1 hydrogen bond · protein-protein
B–F · 310 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

5ZC1 · X-ray diffraction analysis of the CsStefin-1 · the same entry in another collection · chain A against A, TM-score 1.00

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 A6YID9
Elsewhere: RCSB PDB 5ZC1 · PDBe 5ZC1 · UniProt A6YID9

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