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Crystal structure of a GROELK105A mutant

Analyse Crystal structure of a GROELK105A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WSC
Type: protein
Length: 7,336 residues
Chains: 14
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 60 kda chaperonin
UniProt: P0A6F5
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	60 kda chaperonin	protein	524	53% helix, 19% strand	P0A6F5

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	959	0.82	0.84	98	empty
2	782	0.82	0.85	87	empty
3	1022	0.82	0.83	115	empty
4	967	0.80	0.82	96	empty
5	1068	0.80	0.81	96	empty

Interfaces

28 interfaces between chains.

M–N · 1830 Å² buried · 21 hydrogen bonds · protein-protein
H–N · 1798 Å² buried · 22 hydrogen bonds · protein-protein
I–J · 1779 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 1758 Å² buried · 20 hydrogen bonds · protein-protein
H–I · 1756 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

P0A6F5 · AlphaFold monomer V2.0 prediction for 60 kda chaperonin (P0A6F5) · a predicted model of the same protein · chain K against A, TM-score 0.86

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 P0A6F5
Elsewhere: RCSB PDB 4WSC · PDBe 4WSC · UniProt P0A6F5

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