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The crystal structure of zebrafish il-22

Analyse The crystal structure of zebrafish il-22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4O6K
Type: protein
Length: 542 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interleukin 22
UniProt: Q5TLE4
Pockets: 7 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Interleukin 22	protein	136	74% helix, 0% strand	Q5TLE4
C, D	Interleukin 22	protein	135	68% helix, 0% strand	Q5TLE4

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	427	0.63	0.77	68	empty
2	471	0.62	0.76	68	empty
3	153	0.59	0.84	29	empty
4	223	0.58	0.80	28	empty
5	54	0.37	0.79	15	empty

Interfaces

6 interfaces between chains.

B–C · 974 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 954 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 473 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 359 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 19 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

4O6K · The crystal structure of zebrafish IL-22 · 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 Q5TLE4
Elsewhere: RCSB PDB 4O6K · PDBe 4O6K · UniProt Q5TLE4

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