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Crystal structure of a groel D83A/R197A double mutant

Analyse Crystal structure of a groel D83A/R197A double mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WGL
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	943	0.82	0.83	85	empty
2	993	0.81	0.82	112	empty
3	984	0.80	0.82	95	empty
4	854	0.80	0.83	89	empty
5	1157	0.78	0.80	90	empty

Interfaces

28 interfaces between chains.

D–E · 1763 Å² buried · 16 hydrogen bonds · protein-protein
E–F · 1738 Å² buried · 15 hydrogen bonds · protein-protein
M–N · 1735 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 1734 Å² buried · 20 hydrogen bonds · protein-protein
H–N · 1692 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4WGL · Crystal structure of a GroEL D83A/R197A double mutant · the same entry in another collection · chain K against K, 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 P0A6F5
Elsewhere: RCSB PDB 4WGL · PDBe 4WGL · UniProt P0A6F5

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