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The association domain of C. elegans camkii

Analyse The association domain of C. elegans camkii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F86
Type: protein
Length: 903 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein K11E8.1D
EC: 2.7.11.17
UniProt: O62305
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, D, F, H, J, L, N	Hypothetical protein K11E8.1D (EC 2.7.11.17)	protein	129	29% helix, 47% strand	O62305

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	531	0.72	0.80	40	empty
2	531	0.71	0.80	38	empty
3	563	0.71	0.79	44	empty
4	463	0.70	0.80	36	empty
5	435	0.68	0.80	39	empty

Interfaces

7 interfaces between chains.

L–N · 555 Å² buried · 6 hydrogen bonds · protein-protein
H–J · 536 Å² buried · 6 hydrogen bonds · protein-protein
D–F · 533 Å² buried · 5 hydrogen bonds · protein-protein
B–D · 527 Å² buried · 5 hydrogen bonds · protein-protein
J–L · 496 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2F86 · The Association Domain of C. elegans CaMKII · the same entry in another collection · chain N against N, TM-score 1.00
O62305 · AlphaFold monomer V2.0 prediction for CALCIUM/CALMODULIN-dependent protein kinase type II… · a predicted model of the same protein · chain B against A, TM-score 0.95

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 O62305
Elsewhere: RCSB PDB 2F86 · PDBe 2F86 · UniProt O62305

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